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Volumn 1818, Issue 5, 2012, Pages 1374-1377

A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases

Author keywords

EXAFS; Metal coordination; Transmembrane; Transport; X ray spectroscopy; Zinc

Indexed keywords

ADENOSINE TRIPHOSPHATASE; NITROGEN; OXYGEN; P TYPE ZINC ION ADENOSINE TRIPHOSPHATASE; SULFUR; UNCLASSIFIED DRUG; ZINC ION;

EID: 84858737783     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.02.020     Document Type: Article
Times cited : (28)

References (38)
  • 2
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • D.H. Nies Efflux-mediated heavy metal resistance in prokaryotes FEMS Microbiol. Rev. 27 2003 313 339
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 6
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • M. Lu, J. Chai, and D. Fu Structural basis for autoregulation of the zinc transporter YiiP Nat. Struct. Mol. Biol. 16 2009 1063 1067
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1063-1067
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 7
    • 0037565182 scopus 로고    scopus 로고
    • Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus
    • J.M. Argüello, 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
    • Argüello, J.M.1    Mandal, A.K.2    Mana-Capelli, S.3
  • 8
    • 0035954407 scopus 로고    scopus 로고
    • The cysteine-rich amino-terminal domain of ZntA, a Pb(II)/Zn(II)/Cd(II)- translocating ATPase from Escherichia coli, is not essential for its function
    • B. Mitra, and R. Sharma The cysteine-rich amino-terminal domain of ZntA, a Pb(II)/Zn(II)/Cd(II)-translocating ATPase from Escherichia coli, is not essential for its function Biochemistry 40 2001 7694 7699
    • (2001) Biochemistry , vol.40 , pp. 7694-7699
    • Mitra, B.1    Sharma, R.2
  • 11
    • 81255142801 scopus 로고    scopus 로고
    • Bacterial transition metal P(1B)-ATPases: Transport mechanism and roles in virulence
    • J.M. Argüello, M. González-Guerrero, and D. Raimunda Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence Biochemistry 50 2011 9940 9949
    • (2011) Biochemistry , vol.50 , pp. 9940-9949
    • Argüello, J.M.1    González-Guerrero, M.2    Raimunda, D.3
  • 12
    • 35448961704 scopus 로고    scopus 로고
    • GolS controls the response to gold by the hierarchical induction of Salmonella-specific genes that include a CBA efflux-coding operon
    • L.B. Pontel, M.E. Audero, M. Espariz, S.K. Checa, and F.C. Soncini GolS controls the response to gold by the hierarchical induction of Salmonella-specific genes that include a CBA efflux-coding operon Mol. Microbiol. 66 2007 814 825
    • (2007) Mol. Microbiol. , vol.66 , pp. 814-825
    • Pontel, L.B.1    Audero, M.E.2    Espariz, M.3    Checa, S.K.4    Soncini, F.C.5
  • 16
    • 0042208193 scopus 로고    scopus 로고
    • The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate
    • Z. Hou, and B. Mitra The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate J. Biol. Chem. 278 2003 28455 28461
    • (2003) J. Biol. Chem. , vol.278 , pp. 28455-28461
    • Hou, Z.1    Mitra, B.2
  • 18
    • 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
  • 19
    • 33947658924 scopus 로고    scopus 로고
    • Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: Effect on metal selectivity and activity
    • S.J. Dutta, J. Liu, A.J. Stemmler, and B. Mitra Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: effect on metal selectivity and activity Biochemistry 46 2007 3692 3703
    • (2007) Biochemistry , vol.46 , pp. 3692-3703
    • Dutta, S.J.1    Liu, J.2    Stemmler, A.J.3    Mitra, B.4
  • 20
    • 31044446123 scopus 로고    scopus 로고
    • Metal-binding affinity of the transmembrane site in ZntA: Implications for metal selectivity
    • J. Liu, S.J. Dutta, A.J. Stemmler, and B. Mitra Metal-binding affinity of the transmembrane site in ZntA: implications for metal selectivity Biochemistry 45 2006 763 772
    • (2006) Biochemistry , vol.45 , pp. 763-772
    • Liu, J.1    Dutta, S.J.2    Stemmler, A.J.3    Mitra, B.4
  • 22
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 23
    • 79961103204 scopus 로고    scopus 로고
    • A novel zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model
    • C.V. Rosadini, J.D. Gawronski, D. Raimunda, J.M. Arguello, and B.J. Akerley A novel zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model Infect. Immun. 79 2011 3366 3376
    • (2011) Infect. Immun. , vol.79 , pp. 3366-3376
    • Rosadini, C.V.1    Gawronski, J.D.2    Raimunda, D.3    Arguello, J.M.4    Akerley, B.J.5
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0642303383 scopus 로고    scopus 로고
    • Relativistic calculations of spin-dependent x-ray-absorption spectra
    • A.L. Ankudinov, and J.J. Rehr Relativistic calculations of spin-dependent x-ray-absorption spectra Phys. Rev. B: Condens. Matter 56 1997 R1712 R1716
    • (1997) Phys. Rev. B: Condens. Matter , vol.56
    • Ankudinov, A.L.1    Rehr, J.J.2
  • 29
    • 35949022427 scopus 로고
    • Extended x-ray absorption fine structure-its strengths and limitations as a structural tool
    • P.A. Lee, P.H. Citrin, P. Eisenberger, and B.M. Kincaid Extended x-ray absorption fine structure-its strengths and limitations as a structural tool Rev. Mod. Phys. 53 1981 769 806
    • (1981) Rev. Mod. Phys. , vol.53 , pp. 769-806
    • Lee, P.A.1    Citrin, P.H.2    Eisenberger, P.3    Kincaid, B.M.4
  • 30
    • 0029494171 scopus 로고
    • XAFS of dinuclear metal sites in proteins and model compounds
    • S.T., P.J. Riggs-Gelasco, and J.E. Penner-Hahn XAFS of dinuclear metal sites in proteins and model compounds Coord. Chem. Rev. 144 1995 245 286
    • (1995) Coord. Chem. Rev. , vol.144 , pp. 245-286
    • T, S.1    Riggs-Gelasco, P.J.2    Penner-Hahn, J.E.3
  • 31
    • 16344385272 scopus 로고    scopus 로고
    • Metal-binding characteristics of the amino-terminal domain of ZntA: Binding of lead is different compared to cadmium and zinc
    • J. Liu, A.J. Stemmler, J. Fatima, and B. Mitra Metal-binding characteristics of the amino-terminal domain of ZntA: binding of lead is different compared to cadmium and zinc Biochemistry 44 2005 5159 5167
    • (2005) Biochemistry , vol.44 , pp. 5159-5167
    • Liu, J.1    Stemmler, A.J.2    Fatima, J.3    Mitra, B.4
  • 32
    • 0032569167 scopus 로고    scopus 로고
    • The limitations of x-ray absorption spectroscopy for determining the structure of zinc sites in proteins. When is a tetrathiolate not a tetrathiolate?
    • D.L.T. Kimber Clark-Baldwin, Nandakumar Govindaswamy, Eric S. Gruff, J.B. Chongwoo Kim, Stephen A. Koch, and James E. Penner-Hahn The limitations of x-ray absorption spectroscopy for determining the structure of zinc sites in proteins. When is a tetrathiolate not a tetrathiolate? J. Am. Chem. Soc. 120 1998 8401 8409
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8401-8409
    • Kimber Clark-Baldwin, D.L.T.1    Govindaswamy, N.2    Gruff, E.S.3    Chongwoo Kim, J.B.4    Koch, S.A.5    Penner-Hahn, J.E.6
  • 34
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • I.L. Alberts, K. Nadassy, and S.J. Wodak Analysis of zinc binding sites in protein crystal structures Protein Sci. 7 1998 1700 1716
    • (1998) Protein Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 35
    • 0023667724 scopus 로고
    • Slow- and fast-binding inhibitors of thermolysin display different modes of binding: Crystallographic analysis of extended phosphonamidate transition-state analogues
    • H.M. Holden, D.E. Tronrud, A.F. Monzingo, L.H. Weaver, and B.W. Matthews Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues Biochemistry 26 1987 8542 8553
    • (1987) Biochemistry , vol.26 , pp. 8542-8553
    • Holden, H.M.1    Tronrud, D.E.2    Monzingo, A.F.3    Weaver, L.H.4    Matthews, B.W.5
  • 36
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • D.S. Auld Zinc coordination sphere in biochemical zinc sites Biometals 14 2001 271 313
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 38
    • 34748870747 scopus 로고    scopus 로고
    • Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures
    • K. Patel, A. Kumar, and S. Durani Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures Biochim. Biophys. Acta 1774 2007 1247 1253
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1247-1253
    • Patel, K.1    Kumar, A.2    Durani, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.