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Volumn 356, Issue 5, 2006, Pages 1124-1136

Individual metal ligands play distinct functional roles in the zinc sensor Staphylococcus aureus CzrA

Author keywords

Allosteric regulation; Cobalt; Metal sensor; Metalloregulation; Zinc homeostasis

Indexed keywords

ASPARAGINE; ASPARTIC ACID; BACTERIAL PROTEIN; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; LIGAND; METAL ION; PROTEIN CZRA; UNCLASSIFIED DRUG; ZINC;

EID: 32044441204     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.12.019     Document Type: Article
Times cited : (57)

References (39)
  • 1
    • 1842591322 scopus 로고    scopus 로고
    • Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis
    • K.A. McCall, and C.A. Fierke Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis Biochemistry 43 2004 3979 3986
    • (2004) Biochemistry , vol.43 , pp. 3979-3986
    • McCall, K.A.1    Fierke, C.A.2
  • 3
    • 0038349048 scopus 로고    scopus 로고
    • Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators
    • E. Guedon, and J.D. Helmann Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators Mol. Microbiol. 48 2003 495 506
    • (2003) Mol. Microbiol. , vol.48 , pp. 495-506
    • Guedon, E.1    Helmann, J.D.2
  • 4
    • 3543056937 scopus 로고    scopus 로고
    • Selectivity of metal binding and metal-induced stability of Escherichia coli NikR
    • S.C. Wang, A.V. Dias, S.L. Bloom, and D.B. Zamble Selectivity of metal binding and metal-induced stability of Escherichia coli NikR Biochemistry 43 2004 10018 10028
    • (2004) Biochemistry , vol.43 , pp. 10018-10028
    • Wang, S.C.1    Dias, A.V.2    Bloom, S.L.3    Zamble, D.B.4
  • 6
    • 0042624650 scopus 로고    scopus 로고
    • Structure of the manganese-bound manganese transport regulator of Bacillus subtilis
    • A. Glasfeld, E. Guedon, J.D. Helmann, and R.G. Brennan Structure of the manganese-bound manganese transport regulator of Bacillus subtilis Nature Struct. Biol. 10 2003 652 657
    • (2003) Nature Struct. Biol. , vol.10 , pp. 652-657
    • Glasfeld, A.1    Guedon, E.2    Helmann, J.D.3    Brennan, R.G.4
  • 7
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • E. Pohl, J.C. Haller, A. Mijovilovich, W. Meyer-Klaucke, E. Garman, and M.L. Vasil Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator Mol. Microbiol. 47 2003 903 915
    • (2003) Mol. Microbiol. , vol.47 , pp. 903-915
    • Pohl, E.1    Haller, J.C.2    Mijovilovich, A.3    Meyer-Klaucke, W.4    Garman, E.5    Vasil, M.L.6
  • 9
    • 24944453275 scopus 로고    scopus 로고
    • Structural determinants of metal selectivity in prokaryotic metal-responsive transcriptional regulators
    • M.A. Pennella, and D.P. Giedroc Structural determinants of metal selectivity in prokaryotic metal-responsive transcriptional regulators Biometals 18 2005 413 428
    • (2005) Biometals , vol.18 , pp. 413-428
    • Pennella, M.A.1    Giedroc, D.P.2
  • 10
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • L.S. Busenlehner, M.A. Pennella, and D.P. Giedroc The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance FEMS Microbiol. Rev. 27 2003 131 143
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 11
    • 0028027443 scopus 로고
    • Identification of a putative metal binding site in a new family of metalloregulatory proteins
    • W. Shi, J. Wu, and B.P. Rosen Identification of a putative metal binding site in a new family of metalloregulatory proteins J. Biol. Chem. 269 1994 19826 19829
    • (1994) J. Biol. Chem. , vol.269 , pp. 19826-19829
    • Shi, W.1    Wu, J.2    Rosen, B.P.3
  • 12
    • 0027247583 scopus 로고
    • SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: Identification of a Zn-inhibited DNA-protein complex
    • A.P. Morby, J.S. Turner, J.W. Huckle, and N.J. Robinson SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn-inhibited DNA-protein complex Nucl. Acids Res 21 1993 921 925
    • (1993) Nucl. Acids Res , vol.21 , pp. 921-925
    • Morby, A.P.1    Turner, J.S.2    Huckle, J.W.3    Robinson, N.J.4
  • 13
    • 0027535743 scopus 로고
    • Metalloregulated expression of the ars operon
    • J. Wu, and B.P. Rosen Metalloregulated expression of the ars operon J. Biol. Chem. 268 1993 52 58
    • (1993) J. Biol. Chem. , vol.268 , pp. 52-58
    • Wu, J.1    Rosen, B.P.2
  • 14
    • 0031859042 scopus 로고    scopus 로고
    • Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus
    • A. Xiong, and R.K. Jayaswal Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus J. Bacteriol. 180 1998 4024 4029
    • (1998) J. Bacteriol. , vol.180 , pp. 4024-4029
    • Xiong, A.1    Jayaswal, R.K.2
  • 15
    • 0033009421 scopus 로고    scopus 로고
    • ZntR is an autoregulatory protein and negatively regulates the chromosomal zinc resistance operon znt of Staphylococcus aureus
    • V.K. Singh, A. Xiong, T.R. Usgaard, S. Chakrabarti, R. Deora, T.K. Misra, and R.K. Jayaswal ZntR is an autoregulatory protein and negatively regulates the chromosomal zinc resistance operon znt of Staphylococcus aureus Mol. Microbiol. 33 1999 200 207
    • (1999) Mol. Microbiol. , vol.33 , pp. 200-207
    • Singh, V.K.1    Xiong, A.2    Usgaard, T.R.3    Chakrabarti, S.4    Deora, R.5    Misra, T.K.6    Jayaswal, R.K.7
  • 16
    • 0033037505 scopus 로고    scopus 로고
    • Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912
    • M. Kuroda, H. Hayashi, and T. Ohta Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912 Microbiol. Immunol. 43 1999 115 125
    • (1999) Microbiol. Immunol. , vol.43 , pp. 115-125
    • Kuroda, M.1    Hayashi, H.2    Ohta, T.3
  • 17
    • 0034945014 scopus 로고    scopus 로고
    • ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli
    • G. Grass, B. Fan, B.P. Rosen, S. Franke, D.H. Nies, and C. Rensing ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli J. Bacteriol. 183 2001 4664 4667
    • (2001) J. Bacteriol. , vol.183 , pp. 4664-4667
    • Grass, G.1    Fan, B.2    Rosen, B.P.3    Franke, S.4    Nies, D.H.5    Rensing, C.6
  • 18
    • 7744220357 scopus 로고    scopus 로고
    • Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans CH34 and Escherichia coli
    • A. Anton, A. Weltrowski, C.J. Haney, S. Franke, G. Grass, C. Rensing, and D.H. Nies Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans CH34 and Escherichia coli J. Bacteriol. 186 2004 7499 7507
    • (2004) J. Bacteriol. , vol.186 , pp. 7499-7507
    • Anton, A.1    Weltrowski, A.2    Haney, C.J.3    Franke, S.4    Grass, G.5    Rensing, C.6    Nies, D.H.7
  • 21
    • 0027495961 scopus 로고
    • Engineering a cysteine ligand into the zinc binding site of human carbonic anhydrase II
    • L.L. Kiefer, J.F. Krebs, S.A. Paterno, and C.A. Fierke Engineering a cysteine ligand into the zinc binding site of human carbonic anhydrase II Biochemistry 32 1993 9896 9900
    • (1993) Biochemistry , vol.32 , pp. 9896-9900
    • Kiefer, L.L.1    Krebs, J.F.2    Paterno, S.A.3    Fierke, C.A.4
  • 22
    • 0028590042 scopus 로고
    • Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites
    • L.L. Kiefer, and C.A. Fierke Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites Biochemistry 33 1994 15233 15240
    • (1994) Biochemistry , vol.33 , pp. 15233-15240
    • Kiefer, L.L.1    Fierke, C.A.2
  • 23
    • 0031046749 scopus 로고    scopus 로고
    • Zinc site redesign in T4 gene 32 protein: Structure and stability of cobalt(II) complexes formed by wild-type and metal ligand substitution mutants
    • J. Guo, and D.P. Giedroc Zinc site redesign in T4 gene 32 protein: structure and stability of cobalt(II) complexes formed by wild-type and metal ligand substitution mutants Biochemistry 36 1997 730 742
    • (1997) Biochemistry , vol.36 , pp. 730-742
    • Guo, J.1    Giedroc, D.P.2
  • 24
    • 32044435502 scopus 로고    scopus 로고
    • Structural insights into homo- and heterotropic allosteric coupling in the zinc sensor S. aureus CzrA from covalently fused dimers
    • in the press (ja0546828).
    • Lee, S., Arunkumar, A. I., Chen, X., & Giedroc, D. P. (2006). Structural insights into homo- and heterotropic allosteric coupling in the zinc sensor S. aureus CzrA from covalently fused dimers. J. Am. Chem. Soc. 128, in the press (ja0546828).
    • (2006) J. Am. Chem. Soc. , vol.128
    • Lee, S.1    Arunkumar, A.I.2    Chen, X.3    Giedroc, D.P.4
  • 25
    • 0025341169 scopus 로고
    • Characterization of indo-1 and quin-2 as spectroscopic probes for Zn2(+)-protein interactions
    • J.R. Jefferson, J.B. Hunt, and A. Ginsburg Characterization of indo-1 and quin-2 as spectroscopic probes for Zn2(+)-protein interactions Anal. Biochem. 187 1990 328 336
    • (1990) Anal. Biochem. , vol.187 , pp. 328-336
    • Jefferson, J.R.1    Hunt, J.B.2    Ginsburg, A.3
  • 26
    • 0001210274 scopus 로고
    • Four- and five-coordinate cobalt(II) thiolate complexes: Models for the catalytic site of alcohol dehydrogenase
    • D.T. Corwin Jr, R. Fikar, and S.A. Koch Four- and five-coordinate cobalt(II) thiolate complexes: models for the catalytic site of alcohol dehydrogenase Inorg. Chem. 26 1987 3079 3080
    • (1987) Inorg. Chem. , vol.26 , pp. 3079-3080
    • Corwin Jr., D.T.1    Fikar, R.2    Koch, S.A.3
  • 27
    • 0037031290 scopus 로고    scopus 로고
    • Allosteric negative regulation of smt O/P binding of the zinc sensor, SmtB, by metal ions: A coupled equilibrium analysis
    • M.L. VanZile, X. Chen, and D.P. Giedroc Allosteric negative regulation of smt O/P binding of the zinc sensor, SmtB, by metal ions: a coupled equilibrium analysis Biochemistry 41 2002 9776 9786
    • (2002) Biochemistry , vol.41 , pp. 9776-9786
    • Vanzile, M.L.1    Chen, X.2    Giedroc, D.P.3
  • 29
    • 0029662326 scopus 로고    scopus 로고
    • Zn2+-sensing by the cyanobacterial metallothionein repressor SmtB: Different motifs mediate metal-induced protein-DNA dissociation
    • J.S. Turner, P.D. Glands, A.C. Samson, and N.J. Robinson Zn2+-sensing by the cyanobacterial metallothionein repressor SmtB: different motifs mediate metal-induced protein-DNA dissociation Nucl. Acids Res. 24 1996 3714 3721
    • (1996) Nucl. Acids Res. , vol.24 , pp. 3714-3721
    • Turner, J.S.1    Glands, P.D.2    Samson, A.C.3    Robinson, N.J.4
  • 30
    • 0036301096 scopus 로고    scopus 로고
    • Elucidation of primary (α3N) and vestigial (α5) heavy metal-binding sites in Staphylococcus aureus pI258 CadC: Evolutionary implications for metal ion selectivity of ArsR/SmtB metal sensor proteins
    • L.S. Busenlehner, T.C. Weng, J.E. Penner-Hahn, and D.P. Giedroc Elucidation of primary (α3N) and vestigial (α5) heavy metal-binding sites in Staphylococcus aureus pI258 CadC: evolutionary implications for metal ion selectivity of ArsR/SmtB metal sensor proteins J. Mol. Biol. 319 2002 685 701
    • (2002) J. Mol. Biol. , vol.319 , pp. 685-701
    • Busenlehner, L.S.1    Weng, T.C.2    Penner-Hahn, J.E.3    Giedroc, D.P.4
  • 31
    • 21744460226 scopus 로고    scopus 로고
    • Structural and functional characterization of M. tuberculosis CmtR, a Pb(II)/Cd(II)-sensing SmtB/ArsR metalloregulatory repressor
    • Y. Wang, L. Hemmingsen, and D.P. Giedroc Structural and functional characterization of M. tuberculosis CmtR, a Pb(II)/Cd(II)-sensing SmtB/ArsR metalloregulatory repressor Biochemistry 44 2005 8976 8988
    • (2005) Biochemistry , vol.44 , pp. 8976-8988
    • Wang, Y.1    Hemmingsen, L.2    Giedroc, D.P.3
  • 32
    • 0037064122 scopus 로고    scopus 로고
    • A nickel-cobalt-sensing ArsR-SmtB family repressor. Contributions of cytosol and effector binding sites to metal selectivity
    • J.S. Cavet, W. Meng, M.A. Pennella, R.J. Appelhoff, D.P. Giedroc, and N.J. Robinson A nickel-cobalt-sensing ArsR-SmtB family repressor. Contributions of cytosol and effector binding sites to metal selectivity J. Biol. Chem. 277 2002 38441 38448
    • (2002) J. Biol. Chem. , vol.277 , pp. 38441-38448
    • Cavet, J.S.1    Meng, W.2    Pennella, M.A.3    Appelhoff, R.J.4    Giedroc, D.P.5    Robinson, N.J.6
  • 33
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 34
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • P. Kuzmic Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase Anal. Biochem. 237 1996 260 273
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 35
    • 0030919897 scopus 로고    scopus 로고
    • Fluorescent chemosensors for divalent zinc based on zinc finger domains. Enhanced oxidative stability, metal binding affinity, and structural and functional characterization
    • G.K. Walkup, and B. Imperiali Fluorescent chemosensors for divalent zinc based on zinc finger domains. Enhanced oxidative stability, metal binding affinity, and structural and functional characterization J. Am. Chem. Soc. 119 1997 3443 3450
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3443-3450
    • Walkup, G.K.1    Imperiali, B.2
  • 36
    • 0034718523 scopus 로고    scopus 로고
    • The zinc metalloregulatory protein Synechococcus PCC7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry
    • M.L. VanZile, N.J. Cosper, R.A. Scott, and D.P. Giedroc The zinc metalloregulatory protein Synechococcus PCC7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry Biochemistry 39 2000 11818 11829
    • (2000) Biochemistry , vol.39 , pp. 11818-11829
    • Vanzile, M.L.1    Cosper, N.J.2    Scott, R.A.3    Giedroc, D.P.4
  • 37
    • 0037031312 scopus 로고    scopus 로고
    • Structural characterization of distinct α3N and α5 metal sites in the cyanobacterial zinc sensor SmtB
    • M.L. VanZile, X. Chen, and D.P. Giedroc Structural characterization of distinct α3N and α5 metal sites in the cyanobacterial zinc sensor SmtB Biochemistry 41 2002 9765 9775
    • (2002) Biochemistry , vol.41 , pp. 9765-9775
    • Vanzile, M.L.1    Chen, X.2    Giedroc, D.P.3


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