메뉴 건너뛰기




Volumn 425, Issue 13, 2013, Pages 2299-2308

On allosteric modulation of P-type Cu+-ATPases

Author keywords

alternating access; membrane protein; P type ATPase

Indexed keywords

COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 84879126056     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.03.008     Document Type: Review
Times cited : (29)

References (75)
  • 1
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • J.C. Skou The influence of some cations on an adenosine triphosphatase from peripheral nerves Biochim. Biophys. Acta 23 1957 394 401
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 394-401
    • Skou, J.C.1
  • 2
    • 0028140357 scopus 로고
    • P-type ATPases of eukaryotes and bacteria: Sequence analyses and construction of phylogenetic trees
    • M.J. Fagan, and M.H. Saier Jr P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees J. Mol. Evol. 38 1994 57 99
    • (1994) J. Mol. Evol. , vol.38 , pp. 57-99
    • Fagan, M.J.1    Saier, Jr.M.H.2
  • 3
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • K.B. Axelsen, and M.G. Palmgren Evolution of substrate specificities in the P-type ATPase superfamily J. Mol. Evol. 46 1998 84 101
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 4
    • 33646830005 scopus 로고
    • Ion motive ATPases. 1. Ubiquity, properties, and significance to cell function
    • P.L. Pedersen, and E. Carafoli Ion motive ATPases. 1. Ubiquity, properties, and significance to cell function Trends Biochem. Sci. 12 1987 146 150
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 5
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • W. Kuhlbrandt Biology, structure and mechanism of P-type ATPases Nat. Rev., Mol. Cell Biol. 5 2004 282 295
    • (2004) Nat. Rev., Mol. Cell Biol. , vol.5 , pp. 282-295
    • Kuhlbrandt, W.1
  • 7
    • 0000395323 scopus 로고
    • The role of sodium ions in the activation of electrophorus electric organ adenosine triphosphatase
    • R.W. Albers, S. Fahn, and G.J. Koval The role of sodium ions in the activation of electrophorus electric organ adenosine triphosphatase Proc. Natl Acad. Sci. USA 50 1963 474 481
    • (1963) Proc. Natl Acad. Sci. USA , vol.50 , pp. 474-481
    • Albers, R.W.1    Fahn, S.2    Koval, G.J.3
  • 8
    • 13344294802 scopus 로고
    • An enzymatic mechanism of active sodium and potassium transport
    • R.L. Post, and A.K. Sen An enzymatic mechanism of active sodium and potassium transport J. Histochem. Cytochem. 13 1965 105 112
    • (1965) J. Histochem. Cytochem. , vol.13 , pp. 105-112
    • Post, R.L.1    Sen, A.K.2
  • 9
    • 0018401053 scopus 로고
    • 2 +-dependent ATPase of the sarcoplasmic reticulum
    • 2 +-dependent ATPase of the sarcoplasmic reticulum Annu. Rev. Biochem. 48 1979 275 292
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 275-292
    • De Meis, L.1    Vianna, A.L.2
  • 10
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • O. Jardetzky Simple allosteric model for membrane pumps Nature 211 1966 969 970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 13
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Ç resolution
    • C. Toyoshima, M. Nakasako, H. Nomura, and H. Ogawa Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Ç resolution Nature 405 2000 647 655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 14
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • C. Toyoshima, and H. Nomura Structural changes in the calcium pump accompanying the dissociation of calcium Nature 418 2002 605 611
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 15
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • C. Olesen, T.L. Sorensen, R.C. Nielsen, J.V. Moller, and P. Nissen Dephosphorylation of the calcium pump coupled to counterion occlusion Science 306 2004 2251 2255
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sorensen, T.L.2    Nielsen, R.C.3    Moller, J.V.4    Nissen, P.5
  • 16
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • T.L. Sorensen, J.V. Moller, and P. Nissen Phosphoryl transfer and calcium ion occlusion in the calcium pump Science 304 2004 1672 1675
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorensen, T.L.1    Moller, J.V.2    Nissen, P.3
  • 17
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • C. Toyoshima, and T. Mizutani Crystal structure of the calcium pump with a bound ATP analogue Nature 430 2004 529 535
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 18
  • 22
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • J.V. Moller, B. Juul, and M. le Maire Structural organization, ion transport, and energy transduction of P-type ATPases Biochim. Biophys. Acta 1286 1996 1 51
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Le Maire, M.3
  • 23
    • 0037565182 scopus 로고    scopus 로고
    • Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus
    • J.M. Arguello, A.K. Mandal, and S. Mana-Capelli Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus Ann. N. Y. Acad. Sci. 986 2003 212 218
    • (2003) Ann. N. Y. Acad. Sci. , vol.986 , pp. 212-218
    • Arguello, J.M.1    Mandal, A.K.2    Mana-Capelli, S.3
  • 24
    • 77149122885 scopus 로고    scopus 로고
    • Metal trafficking: From maintaining the metal homeostasis to future drug design
    • L.A. Ba, M. Doering, T. Burkholz, and C. Jacob Metal trafficking: from maintaining the metal homeostasis to future drug design Metallomics 1 2009 292 311
    • (2009) Metallomics , vol.1 , pp. 292-311
    • Ba, L.A.1    Doering, M.2    Burkholz, T.3    Jacob, C.4
  • 27
    • 0028866670 scopus 로고
    • Organization of P-type ATPases: Significance of structural diversity
    • S. Lutsenko, and J.H. Kaplan Organization of P-type ATPases: significance of structural diversity Biochemistry 34 1995 15607 15613
    • (1995) Biochemistry , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 28
    • 34248633103 scopus 로고    scopus 로고
    • The structure and function of heavy metal transport P1B-ATPases
    • J.M. Argüello, E. Eren, and M. González-Guerrero The structure and function of heavy metal transport P1B-ATPases Biometals 20 2007 233 248
    • (2007) Biometals , vol.20 , pp. 233-248
    • Argüello, J.M.1    Eren, E.2    González-Guerrero, M.3
  • 29
    • 0141987910 scopus 로고    scopus 로고
    • Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases
    • J.M. Arguello Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases J. Membr. Biol. 195 2003 93 108
    • (2003) J. Membr. Biol. , vol.195 , pp. 93-108
    • Arguello, J.M.1
  • 30
    • 0023656068 scopus 로고
    • Maintenance of intracellular calcium in Escherichia coli
    • P. Gangola, and B.P. Rosen Maintenance of intracellular calcium in Escherichia coli J. Biol. Chem. 262 1987 12570 12574
    • (1987) J. Biol. Chem. , vol.262 , pp. 12570-12574
    • Gangola, P.1    Rosen, B.P.2
  • 31
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • T.D. Rae, P.J. Schmidt, R.A. Pufahl, V.C. Culotta, and T.V. O'Halloran Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase Science 284 1999 805 808
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 32
    • 39749187554 scopus 로고    scopus 로고
    • Copper transport and Alzheimer's disease
    • I.G. Macreadie Copper transport and Alzheimer's disease Eur. Biophys. J. 37 2008 295 300
    • (2008) Eur. Biophys. J. , vol.37 , pp. 295-300
    • Macreadie, I.G.1
  • 34
    • 0036299066 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states
    • L. Banci, I. Bertini, S. Ciofi-Baffoni, M. D'Onofrio, L. Gonnelli, F.C. Marhuenda-Egea, and F.J. Ruiz-Duenas Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states J. Mol. Biol. 317 2002 415 429
    • (2002) J. Mol. Biol. , vol.317 , pp. 415-429
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    D'Onofrio, M.4    Gonnelli, L.5    Marhuenda-Egea, F.C.6    Ruiz-Duenas, F.J.7
  • 35
    • 84859832471 scopus 로고    scopus 로고
    • Structural models of the human copper P-type ATPases ATP7A and ATP7B
    • P. Gourdon, O. Sitsel, J.L. Karlsen, L.B. Moller, and P. Nissen Structural models of the human copper P-type ATPases ATP7A and ATP7B Biol. Chem. 393 2012 205 216
    • (2012) Biol. Chem. , vol.393 , pp. 205-216
    • Gourdon, P.1    Sitsel, O.2    Karlsen, J.L.3    Moller, L.B.4    Nissen, P.5
  • 36
  • 37
    • 80052477751 scopus 로고    scopus 로고
    • The architecture of CopA from Archaeoglobus fulgidus studied by cryo-electron microscopy and computational docking
    • G.S. Allen, C.-C. Wu, T. Cardozo, and David L. Stokes The architecture of CopA from Archaeoglobus fulgidus studied by cryo-electron microscopy and computational docking Structure 19 2011 1219 1232
    • (2011) Structure , vol.19 , pp. 1219-1232
    • Allen, G.S.1    Wu, C.-C.2    Cardozo, T.3    Stokes, D.L.4
  • 38
    • 44649182134 scopus 로고    scopus 로고
    • Structure of a copper pump suggests a regulatory role for its metal-binding domain
    • C.-C. Wu, W.J. Rice, and D.L. Stokes Structure of a copper pump suggests a regulatory role for its metal-binding domain Structure 16 2008 976 985
    • (2008) Structure , vol.16 , pp. 976-985
    • Wu, C.-C.1    Rice, W.J.2    Stokes, D.L.3
  • 40
    • 0037033056 scopus 로고    scopus 로고
    • Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase
    • B. Fan Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase J. Biol. Chem. 277 2002 46987 46992
    • (2002) J. Biol. Chem. , vol.277 , pp. 46987-46992
    • Fan, B.1
  • 42
    • 33750601861 scopus 로고    scopus 로고
    • The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity
    • J. Okkeri, and T. Haltia The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity Biochim. Biophys. Acta 1757 2006 1485 1495
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1485-1495
    • Okkeri, J.1    Haltia, T.2
  • 43
    • 0034705616 scopus 로고    scopus 로고
    • Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2
    • D.L. Huffman, and T.V. O'Halloran Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2 J. Biol. Chem. 275 2000 18611 18614
    • (2000) J. Biol. Chem. , vol.275 , pp. 18611-18614
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 47
    • 84874957001 scopus 로고    scopus 로고
    • Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state
    • C. Toyoshima, S. Iwasawa, H. Ogawa, A. Hirata, J. Tsueda, and G. Inesi Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state Nature 495 2013 260 264
    • (2013) Nature , vol.495 , pp. 260-264
    • Toyoshima, C.1    Iwasawa, S.2    Ogawa, H.3    Hirata, A.4    Tsueda, J.5    Inesi, G.6
  • 49
    • 84865291615 scopus 로고    scopus 로고
    • Flexible P-type ATPases interacting with the membrane
    • L. Thogersen, and P. Nissen Flexible P-type ATPases interacting with the membrane Curr. Opin. Struct. Biol. 22 2012 491 499
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 491-499
    • Thogersen, L.1    Nissen, P.2
  • 50
    • 84859972108 scopus 로고    scopus 로고
    • Metal transport across biomembranes: Emerging models for a distinct chemistry
    • J.M. Arguello, D. Raimunda, and M. Gonzalez-Guerrero Metal transport across biomembranes: emerging models for a distinct chemistry J. Biol. Chem. 287 2012 13510 13517
    • (2012) J. Biol. Chem. , vol.287 , pp. 13510-13517
    • Arguello, J.M.1    Raimunda, D.2    Gonzalez-Guerrero, M.3
  • 52
    • 2442572209 scopus 로고    scopus 로고
    • The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1
    • J.M. Walker, D. Huster, M. Ralle, C.T. Morgan, N.J. Blackburn, and S. Lutsenko The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1 J. Biol. Chem. 279 2004 15376 15384
    • (2004) J. Biol. Chem. , vol.279 , pp. 15376-15384
    • Walker, J.M.1    Huster, D.2    Ralle, M.3    Morgan, C.T.4    Blackburn, N.J.5    Lutsenko, S.6
  • 54
    • 72049117359 scopus 로고    scopus 로고
    • Structural organization of human Cu-transporting ATPases: Learning from building blocks
    • A.N. Barry, U. Shinde, and S. Lutsenko Structural organization of human Cu-transporting ATPases: learning from building blocks J. Biol. Inorg. Chem. 15 2010 47 59
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 47-59
    • Barry, A.N.1    Shinde, U.2    Lutsenko, S.3
  • 55
    • 0041856098 scopus 로고    scopus 로고
    • The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein
    • D. Huster, and S. Lutsenko The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein J. Biol. Chem. 278 2003 32212 32218
    • (2003) J. Biol. Chem. , vol.278 , pp. 32212-32218
    • Huster, D.1    Lutsenko, S.2
  • 63
    • 0032311442 scopus 로고    scopus 로고
    • Structure-function relationships of E1-E2 transitions and cation binding in Na, K-pump protein
    • P.L. Jorgensen, J.M. Nielsen, J.H. Rasmussen, and P.A. Pedersen Structure-function relationships of E1-E2 transitions and cation binding in Na, K-pump protein Biochim. Biophys. Acta 1365 1998 65 70
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 65-70
    • Jorgensen, P.L.1    Nielsen, J.M.2    Rasmussen, J.H.3    Pedersen, P.A.4
  • 65
    • 84255178757 scopus 로고    scopus 로고
    • Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function
    • J.T. Rubino, and K.J. Franz Coordination chemistry of copper proteins: how nature handles a toxic cargo for essential function J. Inorg. Biochem. 107 2012 129 143
    • (2012) J. Inorg. Biochem. , vol.107 , pp. 129-143
    • Rubino, J.T.1    Franz, K.J.2
  • 66
    • 70350627430 scopus 로고    scopus 로고
    • Structural biology of copper trafficking
    • A.K. Boal, and A.C. Rosenzweig Structural biology of copper trafficking Chem. Rev. 109 2009 4760 4779
    • (2009) Chem. Rev. , vol.109 , pp. 4760-4779
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 70
    • 0035834661 scopus 로고    scopus 로고
    • Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein
    • T. Nittis, G.N. George, and D.R. Winge Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein J. Biol. Chem. 276 2001 42520 42526
    • (2001) J. Biol. Chem. , vol.276 , pp. 42520-42526
    • Nittis, T.1    George, G.N.2    Winge, D.R.3
  • 71
    • 33845736364 scopus 로고    scopus 로고
    • CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator
    • T. Liu, A. Ramesh, Z. Ma, S.K. Ward, L.M. Zhang, and G.N. George CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator Nat. Chem. Biol. 3 2007 60 68
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 60-68
    • Liu, T.1    Ramesh, A.2    Ma, Z.3    Ward, S.K.4    Zhang, L.M.5    George, G.N.6
  • 73
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • T.E. Decoursey Voltage-gated proton channels and other proton transfer pathways Physiol. Rev. 83 2003 475 579
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • Decoursey, T.E.1
  • 74
    • 0020967882 scopus 로고
    • Hydrogen bonded chain mechanisms for proton conduction and proton pumping
    • J.F. Nagle, and S. Tristram-Nagle Hydrogen bonded chain mechanisms for proton conduction and proton pumping J. Membr. Biol. 74 1983 1 14
    • (1983) J. Membr. Biol. , vol.74 , pp. 1-14
    • Nagle, J.F.1    Tristram-Nagle, S.2
  • 75
    • 79952265848 scopus 로고    scopus 로고
    • Copper trafficking mechanism of CXXC-containing domains: Insight from the pH-dependence of their Cu(I) affinities
    • A. Badarau, and C. Dennison Copper trafficking mechanism of CXXC-containing domains: insight from the pH-dependence of their Cu(I) affinities J. Am. Chem. Soc. 133 2011 2983 2988
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2983-2988
    • Badarau, A.1    Dennison, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.