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Journal articles on the topic 'ATP – Structure'

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Published: 4 June 2021

Last updated: 10 February 2022

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1

Yan, Yan, X. Zhou, H. Xu, and Karsten Melcher. "Structure and Physiological Regulation of AMPK." International Journal of Molecular Sciences 19, no. 11 (2018): 3534. http://dx.doi.org/10.3390/ijms19113534.

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Adenosine monophosphate (AMP)-activated protein kinase (AMPK) is a heterotrimeric αβγ complex that functions as a central regulator of energy homeostasis. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK’s kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs. AMPK senses the cellular energy state by competitive binding of the three adenine nucleotides AMP, ADP, and ATP to three sites in its γ subunit, each, which in turn modulates the ac

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2

Klingenberg, Martin. "Structure-function of the ADP/ATP carrier." Biochemical Society Transactions 20, no. 3 (1992): 547–50. http://dx.doi.org/10.1042/bst0200547.

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3

Haines, Thomas H. "Cardiolipin's Structure, ATP Synthesis & Barth'S Syndrome." Biophysical Journal 96, no. 3 (2009): 242a. http://dx.doi.org/10.1016/j.bpj.2008.12.1193.

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4

Klingenberg, Martin, and David R. Nelson. "Structure-function relationships of the ADP/ATP carrier." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1187, no. 2 (1994): 241–44. http://dx.doi.org/10.1016/0005-2728(94)90119-8.

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5

Neupane, Prashant, Sudina Bhuju, Nita Thapa, and Hitesh Kumar Bhattarai. "ATP Synthase: Structure, Function and Inhibition." Biomolecular Concepts 10, no. 1 (2019): 1–10. http://dx.doi.org/10.1515/bmc-2019-0001.

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AbstractOxidative phosphorylation is carried out by five complexes, which are the sites for electron transport and ATP synthesis. Among those, Complex V (also known as the F1F0 ATP Synthase or ATPase) is responsible for the generation of ATP through phosphorylation of ADP by using electrochemical energy generated by proton gradient across the inner membrane of mitochondria. A multi subunit structure that works like a pump functions along the proton gradient across the membranes which not only results in ATP synthesis and breakdown, but also facilitates electron transport. Since ATP is the majo

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6

THOMAS, P., M. BIANCHET, D. GARBOCZI, J. HULLIHEN, L. AMZEL, and P. PEDERSEN. "ATP synthase: structure-function relationships." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1101, no. 2 (1992): 228–31. http://dx.doi.org/10.1016/s0005-2728(05)80027-1.

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7

WU, Xueji, Mihiro YANO, Hiroyo WASHIDA, and Hiroshi KIDO. "The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis." Biochemical Journal 378, no. 3 (2004): 793–99. http://dx.doi.org/10.1042/bj20031680.

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The chaperone activity of Hsp70 (70 kDa heat-shock protein) in protein folding and its conformational switch, including oligomeric and monomeric interconversion, are regulated by the hydrolysis of ATP and the ATP–ADP exchange cycle. The crystal structure of human ATPase domain shows two metal-binding sites, the first for ATP binding and a second, in close proximity to the first, whose function remains unknown [Sriram, Osipiuk, Freeman, Morimoto and Joachimiak (1997) Structure 5, 403–414]. In this study, we have characterized the second metal-binding motif by site-directed mutagenesis and the k

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8

Petri, Jessica, Yoshio Nakatani, Martin G. Montgomery, et al. "Structure of F1-ATPase from the obligate anaerobeFusobacterium nucleatum." Open Biology 9, no. 6 (2019): 190066. http://dx.doi.org/10.1098/rsob.190066.

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The crystal structure of the F1-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacteriumFusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F1-ATPases fromCaldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and inMycobacterium smegmatis, which has a very low ATP hydrolytic activity. The βE-subunits in all three enzymes are in the conventional ‘open’ state, and in the case ofC. thermarumandM. smegmatis, they are occupied by an ADP

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9

Ko, Tzu-Ping, Yu-Chuan Wang, Chia-Ling Tsai, Chia-Shin Yang, Mei-Hui Hou, and Yeh Chen. "Crystal structure and functional implication of a bacterial cyclic AMP–AMP–GMP synthetase." Nucleic Acids Research 49, no. 8 (2021): 4725–37. http://dx.doi.org/10.1093/nar/gkab165.

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Abstract Mammalian cyclic GMP-AMP synthase (cGAS) and its homologue dinucleotide cyclase in Vibrio cholerae (VcDncV) produce cyclic dinucleotides (CDNs) that participate in the defense against viral infection. Recently, scores of new cGAS/DncV-like nucleotidyltransferases (CD-NTases) were discovered, which produce various CDNs and cyclic trinucleotides (CTNs) as second messengers. Here, we present the crystal structures of EcCdnD, a CD-NTase from Enterobacter cloacae that produces cyclic AMP-AMP-GMP, in its apo-form and in complex with ATP, ADP and AMPcPP, an ATP analogue. Despite the similar

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10

Clémençon, Benjamin, Martial Rey, Véronique Trézéguet, Eric Forest, and Ludovic Pelosi. "Yeast ADP/ATP Carrier Isoform 2." Journal of Biological Chemistry 286, no. 41 (2011): 36119–31. http://dx.doi.org/10.1074/jbc.m111.277376.

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The mitochondrial ADP/ATP carrier, or Ancp, is a member of the mitochondrial carrier family responsible for exchanging ADP and ATP across the mitochondrial inner membrane. ADP/ATP transport involves Ancp switching between two conformational states. These can be analyzed using specific inhibitors, carboxyatractyloside (CATR) and bongkrekic acid (BA). The high resolution three-dimensional structure of bovine Anc1p (bAnc1p), as a CATR-carrier complex, has been solved. However, because the structure of the BA-carrier complex has not yet been determined, the detailed mechanism of transport remains

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11

Keller, David, Seema Singh, Paola Turina, Roderick Capaldi, and Carlos Bustamante. "Structure of ATP synthase by SFM and single-particle image analysis." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 722–23. http://dx.doi.org/10.1017/s0424820100139986.

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F1Fo ATP synthases are the proteins responsible for the synthesis of ATP in oxidative phosphorylation, and are present in some form in all aerobic organisms, both prokaryotic and eukaryotic. They use the energy stored in a transmembrane proton gradient (which is generated by other members of the oxidative phosphorylation pathway) to synthesize ATP from ADP and Pi or, working in reverse, to pump protons across the membrane using the energy of ATP hydrolysis. The full protein has two sectors, F1 and Fo. F1 is normally bound to Fo (which is membrane integrated), but is water soluble when dissocia

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12

Cusack, Noel, and Susanna Hourani. "Structure-activity relationships of ATP receptors." Japanese Journal of Pharmacology 52 (1990): 3. http://dx.doi.org/10.1016/s0021-5198(19)32884-7.

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13

Couoh-Cardel, Sergio J., Salvador Uribe-Carvajal, Stephan Wilkens, and José J. García-Trejo. "Structure of Dimeric F1F0-ATP Synthase." Journal of Biological Chemistry 285, no. 47 (2010): 36447–55. http://dx.doi.org/10.1074/jbc.m110.144907.

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14

WALKER, JOHN E., ALISON L. COZENS, MARK R. DYER, IAN M. FEARNLEY, STEPHEN J. POWELL, and MICHAEL J. RUNSWICK. "Structure and genes of ATP synthase." Biochemical Society Transactions 15, no. 1 (1987): 104–6. http://dx.doi.org/10.1042/bst0150104.

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15

Walker, John E. "Structure and mechanism of ATP synthase." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1857 (August 2016): e3. http://dx.doi.org/10.1016/j.bbabio.2016.04.018.

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16

Immormino, Robert M., D. Eric Dollins, Paul L. Shaffer, Karen L. Soldano, Melissa A. Walker, and Daniel T. Gewirth. "Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone." Journal of Biological Chemistry 279, no. 44 (2004): 46162–71. http://dx.doi.org/10.1074/jbc.m405253200.

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GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with theN-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleot

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17

Pebay-Peyroula, Eva, Cécile Dahout-Gonzalez, Richard Kahn, Véronique Trézéguet, Guy J. M. Lauquin, and Gérard Brandolin. "Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside." Nature 426, no. 6962 (2003): 39–44. http://dx.doi.org/10.1038/nature02056.

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18

Zhang, Zhe, Fangyu Liu, and Jue Chen. "Molecular structure of the ATP-bound, phosphorylated human CFTR." Proceedings of the National Academy of Sciences 115, no. 50 (2018): 12757–62. http://dx.doi.org/10.1073/pnas.1815287115.

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The cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel important in maintaining proper functions of the lung, pancreas, and intestine. The activity of CFTR is regulated by ATP and protein kinase A-dependent phosphorylation. To understand the conformational changes elicited by phosphorylation and ATP binding, we present here the structure of phosphorylated, ATP-bound human CFTR, determined by cryoelectron microscopy to 3.2-Å resolution. This structure reveals the position of the R domain after phosphorylation. By comparing the structures of human CFTR and zebrafish C

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19

Li, Sheng, Yongcheng Lu, Baozhen Peng, and Jianping Ding. "Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site." Biochemical Journal 401, no. 1 (2006): 39–47. http://dx.doi.org/10.1042/bj20061066.

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PRPP (phosphoribosylpyrophosphate) is an important metabolite essential for nucleotide synthesis and PRS (PRPP synthetase) catalyses synthesis of PRPP from R5P (ribose 5-phosphate) and ATP. The enzymatic activity of PRS is regulated by phosphate ions, divalent metal cations and ADP. In the present study we report the crystal structures of recombinant human PRS1 in complexes with SO42− ions alone and with ATP, Cd2+ and SO42− ions respectively. The AMP moiety of ATP binds at the ATP-binding site, and a Cd2+ ion binds at the active site and in a position to interact with the β- and γ-phosphates o

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20

Kühlbrandt, Werner. "Structure and Mechanisms of F-Type ATP Synthases." Annual Review of Biochemistry 88, no. 1 (2019): 515–49. http://dx.doi.org/10.1146/annurev-biochem-013118-110903.

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F1Fo ATP synthases produce most of the ATP in the cell. F-type ATP synthases have been investigated for more than 50 years, but a full understanding of their molecular mechanisms has become possible only with the recent structures of complete, functionally competent complexes determined by electron cryo-microscopy (cryo-EM). High-resolution cryo-EM structures offer a wealth of unexpected new insights. The catalytic F1 head rotates with the central γ-subunit for the first part of each ATP-generating power stroke. Joint rotation is enabled by subunit δ/OSCP acting as a flexible hinge between F1

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21

Tang, Liang, Haiyan Zhao, Theodore Christensen, Zihan Lin, and Annie Lynn. "Visualizing ATP hydrolysis in a viral DNA-packaging molecular motor." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1604. http://dx.doi.org/10.1107/s2053273314083958.

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Many DNA viruses encode powerful molecular machines to package viral genome into preformed protein shells. These DNA-packaging motors contain an ATPase module that converts the chemical reaction of ATP hydrolysis to physical motion of DNA. We previously determined the structures of the DNA-packaging motor gp2 of Shigella phage Sf6 in the apo form and in complex with ADP and ATP-gamma-S (Zhao et al, 2013, PNAS, 110, 8075). Here we report the structure of gp2 in complex with its substrate ATP at 2.0 Angstrom resolution. To our knowledge, this is the first time to capture, at high resolution, a p

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22

Spikes, Tobias E., Martin G. Montgomery, and John E. Walker. "Structure of the dimeric ATP synthase from bovine mitochondria." Proceedings of the National Academy of Sciences 117, no. 38 (2020): 23519–26. http://dx.doi.org/10.1073/pnas.2013998117.

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The structure of the dimeric ATP synthase from bovine mitochondria determined in three rotational states by electron cryo-microscopy provides evidence that the proton uptake from the mitochondrial matrix via the proton inlet half channel proceeds via a Grotthus mechanism, and a similar mechanism may operate in the exit half channel. The structure has given information about the architecture and mechanical constitution and properties of the peripheral stalk, part of the membrane extrinsic region of the stator, and how the action of the peripheral stalk damps the side-to-side rocking motions tha

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23

Unciuleac, Mihaela-Carmen, Yehuda Goldgur, and Stewart Shuman. "Caveat mutator: alanine substitutions for conserved amino acids in RNA ligase elicit unexpected rearrangements of the active site for lysine adenylylation." Nucleic Acids Research 48, no. 10 (2020): 5603–15. http://dx.doi.org/10.1093/nar/gkaa238.

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Abstract Naegleria gruberi RNA ligase (NgrRnl) exemplifies the Rnl5 family of adenosine triphosphate (ATP)-dependent polynucleotide ligases that seal 3′-OH RNA strands in the context of 3′-OH/5′-PO4 nicked duplexes. Like all classic ligases, NgrRnl forms a covalent lysyl–AMP intermediate. A two-metal mechanism of lysine adenylylation was established via a crystal structure of the NgrRnl•ATP•(Mn2+)2 Michaelis complex. Here we conducted an alanine scan of active site constituents that engage the ATP phosphates and the metal cofactors. We then determined crystal structures of ligase-defective Ngr

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24

Cai, Yongfei, Mingyang Su, Ashfaq Ahmad, et al. "Conformational dynamics of the essential sensor histidine kinase WalK." Acta Crystallographica Section D Structural Biology 73, no. 10 (2017): 793–803. http://dx.doi.org/10.1107/s2059798317013043.

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Two-component systems (TCSs) are key elements in bacterial signal transduction in response to environmental stresses. TCSs generally consist of sensor histidine kinases (SKs) and their cognate response regulators (RRs). Many SKs exhibit autokinase, phosphoryltransferase and phosphatase activities, which regulate RR activity through a phosphorylation and dephosphorylation cycle. However, how SKs perform different enzymatic activities is poorly understood. Here, several crystal structures of the minimal catalytic region of WalK, an essential SK fromLactobacillus plantarumthat shares 60% sequence

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25

Schmidt, Marion, Andrei N. Lupas, and Daniel Finley. "Structure and mechanism of ATP-dependent proteases." Current Opinion in Chemical Biology 3, no. 5 (1999): 584–91. http://dx.doi.org/10.1016/s1367-5931(99)00013-7.

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26

Cho, Yoonsang, Vivek Sharma, and James C. Sacchettini. "Crystal Structure of ATP Phosphoribosyltransferase fromMycobacterium tuberculosis." Journal of Biological Chemistry 278, no. 10 (2003): 8333–39. http://dx.doi.org/10.1074/jbc.m212124200.

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27

Okuno, D., R. Iino, and H. Noji. "Rotation and structure of FoF1-ATP synthase." Journal of Biochemistry 149, no. 6 (2011): 655–64. http://dx.doi.org/10.1093/jb/mvr049.

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28

Schubert, Heidi L., and Christopher P. Hill. "Structure of ATP-Bound Human ATP:Cobalamin Adenosyltransferase†." Biochemistry 45, no. 51 (2006): 15188–96. http://dx.doi.org/10.1021/bi061396f.

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29

Yanyushin, Mikhail F. "Subunit structure of ATP synthase fromchloroflexus aurantiacus." FEBS Letters 335, no. 1 (1993): 85–88. http://dx.doi.org/10.1016/0014-5793(93)80445-z.

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30

Xu, Yibin, Paul D. Carr, Thomas Huber, Subhash G. Vasudevan, and David L. Ollis. "The structure of the PII -ATP complex." European Journal of Biochemistry 268, no. 7 (2001): 2028–37. http://dx.doi.org/10.1046/j.1432-1327.2001.02074.x.

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31

Urosev, Dunja, Qing Ma, Agnes L. C. Tan, Robert C. Robinson, and Leslie D. Burtnick. "The Structure of Gelsolin Bound to ATP." Journal of Molecular Biology 357, no. 3 (2006): 765–72. http://dx.doi.org/10.1016/j.jmb.2006.01.027.

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32

Clarke, M. L., W. Hofman, and J. S. Wray. "ATP binding and crossbridge structure in muscle." Journal of Molecular Biology 191, no. 3 (1986): 581–85. http://dx.doi.org/10.1016/0022-2836(86)90153-1.

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33

Gu, Jinke, Laixing Zhang, Shuai Zong, et al. "Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1." Science 364, no. 6445 (2019): 1068–75. http://dx.doi.org/10.1126/science.aaw4852.

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The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo–electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the A

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34

Esue, Osigwe, Denis Wirtz, and Yiider Tseng. "GTPase Activity, Structure, and Mechanical Properties of Filaments Assembled from Bacterial Cytoskeleton Protein MreB." Journal of Bacteriology 188, no. 3 (2006): 968–76. http://dx.doi.org/10.1128/jb.188.3.968-976.2006.

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ABSTRACT MreB, a major component of the recently discovered bacterial cytoskeleton, displays a structure homologous to its eukaryotic counterpart actin. Here, we study the assembly and mechanical properties of Thermotoga maritima MreB in the presence of different nucleotides in vitro. We found that GTP, not ADP or GDP, can mediate MreB assembly into filamentous structures as effectively as ATP. Upon MreB assembly, both GTP and ATP release the gamma phosphate at similar rates. Therefore, MreB is an equally effective ATPase and GTPase. Electron microscopy and quantitative rheology suggest that t

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35

Nury, H., C. Dahout-Gonzalez, V. Trézéguet, G. J. M. Lauquin, G. Brandolin, and E. Pebay-Peyroula. "Relations Between Structure and Function of the Mitochondrial ADP/ATP Carrier." Annual Review of Biochemistry 75, no. 1 (2006): 713–41. http://dx.doi.org/10.1146/annurev.biochem.75.103004.142747.

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36

Tran, Huyen-Thi, Myoung-Ki Hong, Ho-Phuong-Thuy Ngo, et al. "Structure ofD-alanine-D-alanine ligase fromYersinia pestis: nucleotide phosphate recognition by the serine loop." Acta Crystallographica Section D Structural Biology 72, no. 1 (2016): 12–21. http://dx.doi.org/10.1107/s2059798315021671.

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D-Alanyl-D-alanine is an essential precursor of bacterial peptidoglycan and is synthesized by D-alanine-D-alanine ligase (DDL) with hydrolysis of ATP; this reaction makes DDL an important drug target for the development of antibacterial agents. Five crystal structures of DDL fromYersinia pestis(YpDDL) were determined at 1.7–2.5 Å resolution: apo, AMP-bound, ADP-bound, adenosine 5′-(β,γ-imido)triphosphate-bound, and D-alanyl-D-alanine- and ADP-bound structures. YpDDL consists of three domains, in which four loops, loop 1, loop 2 (the serine loop), loop 3 (the ω-loop) and loop 4, constitute the

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Rempel, S., W. K. Stanek, and D. J. Slotboom. "ECF-Type ATP-Binding Cassette Transporters." Annual Review of Biochemistry 88, no. 1 (2019): 551–76. http://dx.doi.org/10.1146/annurev-biochem-013118-111705.

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Energy-coupling factor (ECF)–type ATP-binding cassette (ABC) transporters catalyze membrane transport of micronutrients in prokaryotes. Crystal structures and biochemical characterization have revealed that ECF transporters are mechanistically distinct from other ABC transport systems. Notably, ECF transporters make use of small integral membrane subunits (S-components) that are predicted to topple over in the membrane when carrying the bound substrate from the extracellular side of the bilayer to the cytosol. Here, we review the phylogenetic diversity of ECF transporters as well as recent str

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Sandall, Christina F., Bjoern K. Ziehr, and Justin A. MacDonald. "ATP-Binding and Hydrolysis in Inflammasome Activation." Molecules 25, no. 19 (2020): 4572. http://dx.doi.org/10.3390/molecules25194572.

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The prototypical model for NOD-like receptor (NLR) inflammasome assembly includes nucleotide-dependent activation of the NLR downstream of pathogen- or danger-associated molecular pattern (PAMP or DAMP) recognition, followed by nucleation of hetero-oligomeric platforms that lie upstream of inflammatory responses associated with innate immunity. As members of the STAND ATPases, the NLRs are generally thought to share a similar model of ATP-dependent activation and effect. However, recent observations have challenged this paradigm to reveal novel and complex biochemical processes to discern NLRs

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Preiss, Laura, Julian D. Langer, Özkan Yildiz, et al. "Structure of the mycobacterial ATP synthase Forotor ring in complex with the anti-TB drug bedaquiline." Science Advances 1, no. 4 (2015): e1500106. http://dx.doi.org/10.1126/sciadv.1500106.

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Multidrug-resistant tuberculosis (MDR-TB) is more prevalent today than at any other time in human history. Bedaquiline (BDQ), a novelMycobacterium-specific adenosine triphosphate (ATP) synthase inhibitor, is the first drug in the last 40 years to be approved for the treatment of MDR-TB. This bactericidal compound targets the membrane-embedded rotor (c-ring) of the mycobacterial ATP synthase, a key metabolic enzyme required for ATP generation. We report the x-ray crystal structures of a mycobacterial c9ring without and with BDQ bound at 1.55- and 1.7-Å resolution, respectively. The structures a

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Takimura, Tetsuo, Kenji Kamata, Kazuhiro Fukasawa та ін. "Structures of the PKC-ι kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533–551 in the C-terminal tail and their roles in ATP binding". Acta Crystallographica Section D Biological Crystallography 66, № 5 (2010): 577–83. http://dx.doi.org/10.1107/s0907444910005639.

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Protein kinase C (PKC) plays an essential role in a wide range of cellular functions. Although crystal structures of the PKC-θ, PKC-ι and PKC-βII kinase domains have previously been determined in complexes with small-molecule inhibitors, no structure of a PKC–substrate complex has been determined. In the previously determined PKC-ι complex, residues 533–551 in the C-terminal tail were disordered. In the present study, crystal structures of the PKC-ι kinase domain in its ATP-bound and apo forms were determined at 2.1 and 2.0 Å resolution, respectively. In the ATP complex, the electron density o

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41

Katchanov, G., J. Xu, A. Clay, and A. Pelleg. "Electrophysiological-anatomic correlates of ATP-triggered vagal reflex in the dog. IV. Role of LV vagal afferents." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 4 (1997): H1898—H1903. http://dx.doi.org/10.1152/ajpheart.1997.272.4.h1898.

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The negative chronotropic action and the time to peak effect (t(p)) of ATP and its related analogs [2-methylthio-ATP (2-MeSATP), alpha,beta-methylene-ATP (alpha,beta-mATP), and beta,gamma-methylene-ATP (beta,gamma-mATP)] as well as ADP, AMP, and adenosine were determined in anesthetized dogs. Intra-right atrium (RA) and intra-left main coronary artery (LM) ATP markedly suppressed sinus node automaticity. ATP induced a much greater response when administered into the LM than into the RA. The t(p) of ATP administered at the former site was much shorter than that at the latter site. Intra-LM aden

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42

Tang, Dong-Xin, Hai-Ping Zhao, Chun-Shui Pan, et al. "QiShenYiQi Pills, a Compound Chinese Medicine, Ameliorates Doxorubicin-Induced Myocardial Structure Damage and Cardiac Dysfunction in Rats." Evidence-Based Complementary and Alternative Medicine 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/480597.

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QiShenYiQi Pills (QSYQ) is a compound Chinese medicine used for treatment of cardiovascular diseases. The present study investigated the effects of QSYQ on the Doxorubicin- (DOX-) induced disorders in rat cardiac structure and function and the possible mechanism underlying. A total of 24 male Sprague-Dawley rats were administrated by intraperitoneal injections with DOX at a dose of 2.5 mg/kg, once every day for a total of 6 times. After the 6th injection, the rats were evaluated by echocardiographic analysis, and the animals with injured heart(n=14)were divided into 2 groups and further treate

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Linder, Jürgen U. "Structure–function relationships in Escherichia coli adenylate cyclase." Biochemical Journal 415, no. 3 (2008): 449–54. http://dx.doi.org/10.1042/bj20080350.

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Class I adenylate cyclases are found in γ- and δ-proteobacteria. They play central roles in processes such as catabolite repression in Escherichia coli or development of full virulence in pathogens such as Yersinia enterocolitica and Vibrio vulnificus. The catalytic domain (residues 2–446) of the adenylate cyclase of E. coli was overexpressed and purified. It displayed a Vmax of 665 nmol of cAMP·mg−1·min−1 and a Km of 270 μM. Titration of the metal cofactor Mg2+ against the substrate ATP showed a requirement for free metal ions in addition to the MgATP complex, suggesting a two-metal-ion mecha

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Haffke, Matthias, Anja Menzel, Yvonne Carius, Dieter Jahn, and Dirk W. Heinz. "Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides." Acta Crystallographica Section D Biological Crystallography 66, no. 9 (2010): 979–87. http://dx.doi.org/10.1107/s0907444910028593.

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The human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg2+ and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized N

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45

BORMAN, STU. "High-resolution structure obtained for ATP synthesis enzyme." Chemical & Engineering News 72, no. 36 (1994): 31–32. http://dx.doi.org/10.1021/cen-v072n036.p031.

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WEBER, J. "ATP synthase – the structure of the stator stalk." Trends in Biochemical Sciences 32, no. 2 (2007): 53–56. http://dx.doi.org/10.1016/j.tibs.2006.12.006.

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Locher, Kaspar P. "Structure and mechanism of ATP-binding cassette transporters." Philosophical Transactions of the Royal Society B: Biological Sciences 364, no. 1514 (2008): 239–45. http://dx.doi.org/10.1098/rstb.2008.0125.

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ATP-binding cassette (ABC) transporters constitute a large superfamily of integral membrane proteins that includes both importers and exporters. In recent years, several structures of complete ABC transporters have been determined by X-ray crystallography. These structures suggest a mechanism by which binding and hydrolysis of ATP by the cytoplasmic, nucleotide-binding domains control the conformation of the transmembrane domains and therefore which side of the membrane the translocation pathway is exposed to. A basic, conserved two-state mechanism can explain active transport of both ABC impo

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Cloherty, Erin K., Stephanie Hamill, Kara Levine, and Anthony Carruthers. "Sugar Transporter Regulation by ATP and Quaternary Structure." Blood Cells, Molecules, and Diseases 27, no. 1 (2001): 102–7. http://dx.doi.org/10.1006/bcmd.2000.0358.

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Mukai, Takako, Shigeyuki Kawai, Shigetarou Mori, Bunzo Mikami, and Kousaku Murata. "Crystal Structure of Bacterial Inorganic Polyphosphate/ATP-glucomannokinase." Journal of Biological Chemistry 279, no. 48 (2004): 50591–600. http://dx.doi.org/10.1074/jbc.m408126200.

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Flagg, Thomas P., Harley T. Kurata, Ricard Masia, et al. "Differential Structure of Atrial and Ventricular K ATP." Circulation Research 103, no. 12 (2008): 1458–65. http://dx.doi.org/10.1161/circresaha.108.178186.

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