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Volumn 368, Issue 5, 2007, Pages 1358-1366

Crystal Structure of the Zinc-binding Transport Protein ZnuA from Escherichia coli Reveals an Unexpected Variation in Metal Coordination

Author keywords

ABC type transporter system; metal uptake; solute binding protein; X ray crystallography; zinc

Indexed keywords

ESCHERICHIA COLI PROTEIN; GLUTAMIC ACID; HISTIDINE; METAL; PROTEIN ZNUA; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 34247269203     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.107     Document Type: Article
Times cited : (63)

References (39)
  • 1
    • 28644437016 scopus 로고    scopus 로고
    • A bacterial view of the periodic table: genes and proteins for toxic inorganic ions
    • Silver S., and Phung L.T. A bacterial view of the periodic table: genes and proteins for toxic inorganic ions. J. Indust. Microbiol. Biotechnol. 32 (2005) 587-605
    • (2005) J. Indust. Microbiol. Biotechnol. , vol.32 , pp. 587-605
    • Silver, S.1    Phung, L.T.2
  • 2
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies D.H. 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
  • 3
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCs: a phylogenetic and functional classification of ABC systems in living organisms
    • Dassa E., and Bouige P. The ABC of ABCs: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 152 (2001) 211-229
    • (2001) Res. Microbiol. , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, P.2
  • 5
    • 0034635468 scopus 로고    scopus 로고
    • The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli
    • Sharma R., Rensing C., Rosen B.P., and Mitra B. The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli. J. Biol. Chem. 275 (2000) 3873-3878
    • (2000) J. Biol. Chem. , vol.275 , pp. 3873-3878
    • Sharma, R.1    Rensing, C.2    Rosen, B.P.3    Mitra, B.4
  • 6
    • 0030883174 scopus 로고    scopus 로고
    • Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase
    • Beard S.J., Hashim R., MembrilloHernandez J., Hughes M.N., and Poole R.K. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase. Mol. Microbiol. 25 (1997) 883-891
    • (1997) Mol. Microbiol. , vol.25 , pp. 883-891
    • Beard, S.J.1    Hashim, R.2    MembrilloHernandez, J.3    Hughes, M.N.4    Poole, R.K.5
  • 8
    • 0034945014 scopus 로고    scopus 로고
    • ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli
    • Grass G., Fan B., Rosen B.P., Franke S., Nies D. H., and Rensing C. 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
  • 9
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator zur in Escherichia coli
    • Patzer S.I., and Hantke K. The ZnuABC high-affinity zinc uptake system and its regulator zur in Escherichia coli. Mol. Microbiol. 28 (1998) 1199-1210
    • (1998) Mol. Microbiol. , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 10
    • 0034637471 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli
    • Patzer S.I., and Hantke K. The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli. J. Biol. Chem. 275 (2000) 24321-24332
    • (2000) J. Biol. Chem. , vol.275 , pp. 24321-24332
    • Patzer, S.I.1    Hantke, K.2
  • 11
    • 14244251491 scopus 로고    scopus 로고
    • The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum
    • Grass G., Franke S., Taudte N., Nies D.H., Kucharski L.M., Maguire M.E., and Rensing C. The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum. J. Bacteriol. 187 (2005) 1604-1611
    • (2005) J. Bacteriol. , vol.187 , pp. 1604-1611
    • Grass, G.1    Franke, S.2    Taudte, N.3    Nies, D.H.4    Kucharski, L.M.5    Maguire, M.E.6    Rensing, C.7
  • 13
    • 0035696323 scopus 로고    scopus 로고
    • Bacterial zinc transporters and regulators
    • Hantke K. Bacterial zinc transporters and regulators. Biometals 14 (2001) 239-249
    • (2001) Biometals , vol.14 , pp. 239-249
    • Hantke, K.1
  • 14
    • 15744394198 scopus 로고    scopus 로고
    • Bacterial zinc uptake and regulators
    • Hantke K. Bacterial zinc uptake and regulators. Curr. Opin. Microbiol. 8 (2005) 196-202
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 196-202
    • Hantke, K.1
  • 15
    • 0030868591 scopus 로고    scopus 로고
    • Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases
    • Dintilhac A., Alloing G., Granadel C., and Claverys J.P. Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol. Microbiol. 25 (1997) 727-739
    • (1997) Mol. Microbiol. , vol.25 , pp. 727-739
    • Dintilhac, A.1    Alloing, G.2    Granadel, C.3    Claverys, J.P.4
  • 16
    • 0035822583 scopus 로고    scopus 로고
    • Identification and characterization of a high-affinity zinc uptake system in Neisseria gonorrhoeae
    • Chen C.Y., and Morse S.A. Identification and characterization of a high-affinity zinc uptake system in Neisseria gonorrhoeae. FEMS Microbiol. Letters 202 (2001) 67-71
    • (2001) FEMS Microbiol. Letters , vol.202 , pp. 67-71
    • Chen, C.Y.1    Morse, S.A.2
  • 18
    • 0035011106 scopus 로고    scopus 로고
    • A new family of high-affinity ABC manganese and zinc permeases
    • Claverys J.P. A new family of high-affinity ABC manganese and zinc permeases. Res. Microbiol. 152 (2001) 231-243
    • (2001) Res. Microbiol. , vol.152 , pp. 231-243
    • Claverys, J.P.1
  • 19
    • 0032534754 scopus 로고    scopus 로고
    • The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein
    • Lawrence M.C., Pilling P.A., Epa V.C., Berry A.M., Ogunniyi A.D., and Paton J.C. The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein. Structure 6 (1998) 1553-1561
    • (1998) Structure , vol.6 , pp. 1553-1561
    • Lawrence, M.C.1    Pilling, P.A.2    Epa, V.C.3    Berry, A.M.4    Ogunniyi, A.D.5    Paton, J.C.6
  • 20
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee Y.H., Deka R.K., Norgard M.V., Radolf J.D., and Hasemann C.A. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone. Nature Struct. Biol. 6 (1999) 628-633
    • (1999) Nature Struct. Biol. , vol.6 , pp. 628-633
    • Lee, Y.H.1    Deka, R.K.2    Norgard, M.V.3    Radolf, J.D.4    Hasemann, C.A.5
  • 21
    • 0142216623 scopus 로고    scopus 로고
    • Structural determinants of metal specificity in the zinc transport protein ZnuA from Synechocystis 6803
    • Banerjee S., Wei B.X., Bhattacharyya-Pakrasi M., Pakrasi H.B., and Smith T.J. Structural determinants of metal specificity in the zinc transport protein ZnuA from Synechocystis 6803. J. Mol. Biol. 333 (2003) 1061-1069
    • (2003) J. Mol. Biol. , vol.333 , pp. 1061-1069
    • Banerjee, S.1    Wei, B.X.2    Bhattacharyya-Pakrasi, M.3    Pakrasi, H.B.4    Smith, T.J.5
  • 22
    • 0036209769 scopus 로고    scopus 로고
    • The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation
    • Lee Y.H., Dorwart M.R., Hazlett K.R.O., Deka R. K., Norgard M.V., Radolf J.D., and Hasemann C.A. The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation. J. Bacteriol. 184 (2002) 2300-2304
    • (2002) J. Bacteriol. , vol.184 , pp. 2300-2304
    • Lee, Y.H.1    Dorwart, M.R.2    Hazlett, K.R.O.3    Deka, R. K.4    Norgard, M.V.5    Radolf, J.D.6    Hasemann, C.A.7
  • 23
    • 17544376193 scopus 로고    scopus 로고
    • The MntC crystal structure suggests that import of Mn2+ in cyanobacteria is redox controlled
    • Rukhman V., Anati R., Melamed-Frank M., and Adir N. The MntC crystal structure suggests that import of Mn2+ in cyanobacteria is redox controlled. J. Mol. Biol. 348 (2005) 961-969
    • (2005) J. Mol. Biol. , vol.348 , pp. 961-969
    • Rukhman, V.1    Anati, R.2    Melamed-Frank, M.3    Adir, N.4
  • 25
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallog. sect. D 56 (2000) 965-972
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374 (2003) 229-244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 29
    • 27244446613 scopus 로고    scopus 로고
    • Type I signal peptidase: an overview
    • Tuteja R. Type I signal peptidase: an overview. Arch. Biochem. Biophys. 441 (2005) 107-111
    • (2005) Arch. Biochem. Biophys. , vol.441 , pp. 107-111
    • Tuteja, R.1
  • 30
    • 0346118916 scopus 로고    scopus 로고
    • Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli
    • Heddle J., Scott D.J., Unzai S., Park S.Y., and Tame J.R.H. Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli. J. Biol. Chem. 278 (2003) 50322-50329
    • (2003) J. Biol. Chem. , vol.278 , pp. 50322-50329
    • Heddle, J.1    Scott, D.J.2    Unzai, S.3    Park, S.Y.4    Tame, J.R.H.5
  • 31
    • 0030710149 scopus 로고    scopus 로고
    • Identification of the key protein for zinc uptake in Hemophilus influenzae
    • Lu D.S., Boyd B., and Lingwood C.A. Identification of the key protein for zinc uptake in Hemophilus influenzae. J. Biol. Chem. 272 (1997) 29033-29038
    • (1997) J. Biol. Chem. , vol.272 , pp. 29033-29038
    • Lu, D.S.1    Boyd, B.2    Lingwood, C.A.3
  • 32
    • 0027440362 scopus 로고
    • Protein-structure comparison by alignment of distance matrices
    • Holm L., and Sander C. Protein-structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 33
    • 0038081029 scopus 로고    scopus 로고
    • The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase
    • Hazlett K.R.O., Rusnak F., Kehres D.G., Bearden S. W., La Vake C.J., La Vake M.E., et al. The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase. J. Biol. Chem. 278 (2003) 20687-20694
    • (2003) J. Biol. Chem. , vol.278 , pp. 20687-20694
    • Hazlett, K.R.O.1    Rusnak, F.2    Kehres, D.G.3    Bearden, S. W.4    La Vake, C.J.5    La Vake, M.E.6
  • 34
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD) - a vehicle for direct determination of 3-dimensional structure
    • Hendrickson W.A., Horton J.R., and Lemaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD) - a vehicle for direct determination of 3-dimensional structure. EMBO J. 9 (1990) 1665-1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 37
    • 0028103275 scopus 로고
    • The CCP4 Suite: programs for protein crystallography
    • CCP4. The CCP4 Suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
    • CCP41
  • 38
    • 0027968068 scopus 로고
    • Clustal-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. Clustal-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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