메뉴 건너뛰기




Volumn 97, Issue 6, 2009, Pages 1756-1764

Changes in electrostatic surface potential of Na+/K +-ATPase cytoplasmic headpiece induced by cytoplasmic ligand(s) binding

Author keywords

[No Author keywords available]

Indexed keywords

ACRYLAMIDE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; CATION; IODIDE; MAGNESIUM ION; MUTANT PROTEIN; TRYPTOPHAN;

EID: 70350031203     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.07.002     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0041821836 scopus 로고    scopus 로고
    • A perspective on enzyme catalysis
    • Benkovic, S. J., and S. Hammes-Schiffer. 2003. A perspective on enzyme catalysis. Science. 301:1196-1202.
    • (2003) Science , vol.301 , pp. 1196-1202
    • Benkovic, S.J.1    Hammes-Schiffer, S.2
  • 2
    • 58749093927 scopus 로고    scopus 로고
    • Conformational transition pathways explored by Monte Carlo simulation integrated with collective modes
    • Kantarci-Carsibasi, N., T. Haliloglu, and P. Doruker. 2008. Conformational transition pathways explored by Monte Carlo simulation integrated with collective modes. Biophys. J. 95:5862-5873.
    • (2008) Biophys. J. , vol.95 , pp. 5862-5873
    • Kantarci-Carsibasi, N.1    Haliloglu, T.2    Doruker, P.3
  • 3
    • 58149359858 scopus 로고    scopus 로고
    • Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis
    • Wen, P. C., and E. Tajkhorshid. 2008. Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis. Biophys. J. 95:5100-5110.
    • (2008) Biophys. J. , vol.95 , pp. 5100-5110
    • Wen, P.C.1    Tajkhorshid, E.2
  • 4
    • 0038621773 scopus 로고    scopus 로고
    • Structure and mechanism of Na,K-ATPase: Functional sites and their interactions
    • Jorgensen, P. L., K. O. Hakansson, and S. J. D. Karlish. 2003. Structure and mechanism of Na,K-ATPase: Functional sites and their interactions. Annu. Rev. Physiol. 65:817-849.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 817-849
    • Jorgensen, P.L.1    Hakansson, K.O.2    Karlish, S.J.D.3
  • 5
    • 0036385728 scopus 로고    scopus 로고
    • Oligomerization of a peptide derived from the transmembrane region of the sodium pump gamma subunit: Effect of the pathological mutation G41R
    • Therien, A. G., and C.M.Deber. 2002.Oligomerization of a peptide derived from the transmembrane region of the sodium pump gamma subunit: effect of the pathological mutation G41R. J. Mol. Biol. 322:583-590.
    • (2002) J. Mol. Biol. , vol.322 , pp. 583-590
    • Therien, A.G.1    Deber, C.M.2
  • 7
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Moller, J. V., B. Juul, and M. leMaire. 1996. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta. 1286:1-51.
    • (1996) Biochim. Biophys. Acta. , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Lemaire, M.3
  • 9
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • DOI 10.1038/35015017
    • Toyoshima, C., M. Nakasako, H. Nomura, and H. Ogawa. 2000. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 angstrom resolution. Nature. 405:647-655. (Pubitemid 30428644)
    • (2000) Nature , vol.405 , Issue.6787 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 10
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • DOI 10.1038/nature00944
    • Toyoshima, C., and H. Nomura. 2002. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature. 418:605-611. (Pubitemid 34886857)
    • (2002) Nature , vol.418 , Issue.6898 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 11
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • DOI 10.1038/nature02981
    • Toyoshima, C., H. Nomura, and T. Tsuda. 2004. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature. 432:361-368. (Pubitemid 39555518)
    • (2004) Nature , vol.432 , Issue.7015 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 12
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • DOI 10.1038/nature02680
    • Toyoshima, C., and T. Mizutani. 2004. Crystal structure of the calcium pump with a bound ATP analogue. Nature. 430:529-535. (Pubitemid 38998620)
    • (2004) Nature , vol.430 , Issue.6999 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 13
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • DOI 10.1126/science.1099366
    • Sorensen, T. L. M., J. V. Moller, and P. Nissen. 2004. Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science. 304:1672-1675. (Pubitemid 38765859)
    • (2004) Science , vol.304 , Issue.5677 , pp. 1672-1675
    • Sorensen, T.L.-M.1    Moller, J.V.2    Nissen, P.3
  • 15
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • DOI 10.1126/science.1106289
    • Olesen, C., T. L. M. Sorensen, R. C. Nielsen, J. V. Moller, and P. Nissen. 2004. Dephosphorylation of the calcium pump coupled to counterion occlusion. Science. 306:2251-2255. (Pubitemid 40024461)
    • (2004) Science , vol.306 , Issue.5705 , pp. 2251-2255
    • Olesen, C.1    Sorensen, T.L.-M.2    Nielsen, R.C.3    Moller, J.V.4    Nissen, P.5
  • 16
    • 33745762313 scopus 로고    scopus 로고
    • Modulatory and catalytic modes of ATP binding by the calcium pump
    • Jensen, A.M.L., T. L.M.Sorensen, C.Olesen, J. V.Moller, and P. Nissen. 2006. Modulatory and catalytic modes of ATP binding by the calcium pump. EMBO J. 25:2305-2314.
    • (2006) EMBO J , vol.25 , pp. 2305-2314
    • Jensen, A.M.L.1    Sorensen, T.L.M.2    Olesen, C.3    Moller, J.V.4    Nissen, P.5
  • 20
    • 0032562606 scopus 로고    scopus 로고
    • The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein
    • Gatto, C., A. X. Wang, and J. H. Kaplan. 1998. The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein. J. Biol. Chem. 273:10578-10585.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10578-10585
    • Gatto, C.1    Wang, A.X.2    Kaplan, J.H.3
  • 22
    • 0043208929 scopus 로고    scopus 로고
    • Limitations in linearized analyses of binding equilibria: Binding of TNP-ATP to the H-4-H-5 loop of Na/K-ATPase
    • Kubala, M., J. Plasek, and E. Amler. 2003. Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H-4-H-5 loop of Na/K-ATPase. Eur. Biophys. J. Biophys. Lett. 32:363-369.
    • (2003) Eur. Biophys. J. Biophys. Lett. , vol.32 , pp. 363-369
    • Kubala, M.1    Plasek, J.2    Amler, E.3
  • 27
    • 0022401765 scopus 로고
    • Electrostatic interactions in sperm whale myoglobin - Site specificity, roles in structural elements, and external electrostatic potential distributions
    • Garciamoreno, B., L. X. Chen, K. L. March, R. S. Gurd, and F. R. N. Gurd. 1985. Electrostatic interactions in sperm whale myoglobin - site specificity, roles in structural elements, and external electrostatic potential distributions. J. Biol. Chem. 260:4070-4082.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4070-4082
    • Garciamoreno, B.1    Chen, L.X.2    March, K.L.3    Gurd, R.S.4    Gurd, F.R.N.5
  • 33
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner, M. F. 1999. Python: a programming language for software integration and development. J. Mol. Graph. 17:57-61.
    • (1999) J. Mol. Graph. , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 34
    • 33744831751 scopus 로고    scopus 로고
    • ATP-binding to P-type ATPases as revealed by biochemical, spectroscopic, and crystallographic experiments
    • DOI 10.1002/prot.20969
    • Kubala, M. 2006. ATP-binding to P-type ATPases as revealed by biochemical, spectroscopic, and crystallographic experiments. Proteins. 64:1-12. (Pubitemid 43830979)
    • (2006) Proteins: Structure, Function and Genetics , vol.64 , Issue.1 , pp. 1-12
    • Kubala, M.1
  • 36
    • 21444458507 scopus 로고    scopus 로고
    • 2+-ATPase with bound nucleotide differs from that adopted with the transition state analog ADP center dot AlFx or with AMPPCP under crystallization conditions at milli-molar
    • 2+-ATPase with bound nucleotide differs from that adopted with the transition state analog ADP center dot AlFx or with AMPPCP under crystallization conditions at milli-molar. J. Biol. Chem. 280:18745-18754.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18745-18754
    • Picard, M.1    Toyoshima, C.2    Champeil, P.3
  • 37
    • 62649166490 scopus 로고    scopus 로고
    • Changes in negative charge at the luminal mouth of the pore alter ion handling and gating in the cardiac ryanodine-receptor
    • Mead-Savery, F. C., R. Wang, B. Tanna-Topan, S. R. W. Chen, W. Welch, et al. 2009. Changes in negative charge at the luminal mouth of the pore alter ion handling and gating in the cardiac ryanodine-receptor. Biophys. J. 96:1374-1387.
    • (2009) Biophys. J. , vol.96 , pp. 1374-1387
    • Mead-Savery, F.C.1    Wang, R.2    Tanna-Topan, B.3    Chen, S.R.W.4    Welch, W.5
  • 38
    • 0029900085 scopus 로고    scopus 로고
    • Negative electrostatic surface potential of protein sites specific for anionic ligands
    • Ledvina, P. S., N. H. Yao, A. Choudhary, and F. A. Quiocho. 1996. Negative electrostatic surface potential of protein sites specific for anionic ligands. Proc. Natl. Acad. Sci. USA. 93:6786-6791.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6786-6791
    • Ledvina, P.S.1    Yao, N.H.2    Choudhary, A.3    Quiocho, F.A.4
  • 39
    • 11144226220 scopus 로고    scopus 로고
    • 2+ interaction and phosphoenzyme processing
    • 2+ interaction and phosphoenzyme processing. J. Biol. Chem. 279:54426-54437.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54426-54437
    • Clausen, J.D.1    Andersen, J.P.2
  • 40
    • 8544243529 scopus 로고    scopus 로고
    • The role of loop 6/7 in folding and functional performance of Na,K-ATPase
    • Xu, G. Y., D. J. Kane, L. D. Faller, and R. A. Farley. 2004. The role of loop 6/7 in folding and functional performance of Na,K-ATPase. J. Biol. Chem. 279:45594-45602.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45594-45602
    • Xu, G.Y.1    Kane, D.J.2    Faller, L.D.3    Farley, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.