메뉴 건너뛰기




Volumn 333, Issue 5, 2003, Pages 1061-1069

Structural determinants of metal specificity in the zinc transport protein ZnuA from Synechocystis 6803

Author keywords

Crystallography; Metal; Specificity; Transport; Zinc

Indexed keywords

METAL; PROTEIN; PROTEIN ZNUA; UNCLASSIFIED DRUG; ZINC;

EID: 0142216623     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.008     Document Type: Article
Times cited : (98)

References (37)
  • 1
    • 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
  • 2
    • 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
  • 4
    • 0029975786 scopus 로고    scopus 로고
    • Manganese transport in the cyanobacterium Synechocystis sp. PCC 6803
    • Bartsevich V.V., Pakrasi H.B. Manganese transport in the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 271:1996;26057-26061.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26057-26061
    • Bartsevich, V.V.1    Pakrasi, H.B.2
  • 5
    • 0036795485 scopus 로고    scopus 로고
    • Phylogenetic and functional classification of ATP-binding cassette (ABC) systems
    • Bouige P., Laurent D., Piloyan L., Dassa E. Phylogenetic and functional classification of ATP-binding cassette (ABC) systems. Curr. Protein Pept. Sci. 3:2002;541-559.
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 541-559
    • Bouige, P.1    Laurent, D.2    Piloyan, L.3    Dassa, E.4
  • 6
    • 0008281891 scopus 로고    scopus 로고
    • Transport of metals: A key process in oxygenic photosynthesis
    • E.-M. Aro, & B.A. Andersson. Dordrecht, The Netherlands: Kluwer Academic
    • Pakrasi H.B., Ogawa T., Bhattacharyya-Pakrasi M. Transport of metals: a key process in oxygenic photosynthesis. Aro E.-M., Andersson B.A. Regulatory Aspects of Photosynthesis. 2001;253-264 Kluwer Academic, Dordrecht, The Netherlands.
    • (2001) Regulatory Aspects of Photosynthesis , pp. 253-264
    • Pakrasi, H.B.1    Ogawa, T.2    Bhattacharyya-Pakrasi, M.3
  • 7
    • 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., 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
  • 8
    • 0032799345 scopus 로고    scopus 로고
    • Physicochemical evidence that Treponema pallidum TroA is a zinc-containing metalloprotein that lacks porin-like structure
    • Deka R.K., Lee Y.H., Hagman K.E., Shevchenko D., Lingwood C.A., Hasemann C.A., et al. Physicochemical evidence that Treponema pallidum TroA is a zinc-containing metalloprotein that lacks porin-like structure. J. Bacteriol. 181:1999;4420-4423.
    • (1999) J. Bacteriol. , vol.181 , pp. 4420-4423
    • Deka, R.K.1    Lee, Y.H.2    Hagman, K.E.3    Shevchenko, D.4    Lingwood, C.A.5    Hasemann, C.A.6
  • 9
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee Y.-H., Deka R., Norgard M.V., Radolf J.D., 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.2    Norgard, M.V.3    Radolf, J.D.4    Hasemann, C.A.5
  • 10
    • 0036209769 scopus 로고    scopus 로고
    • The crystal structure of a 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., Hasemann C.A. The crystal structure of a 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
  • 11
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer S.I., 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
  • 12
    • 0035822583 scopus 로고    scopus 로고
    • Identification and characterization of a high-affinity zinc uptake system in Neisseria gonorrhoeae
    • Chen C.Y., 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
  • 14
    • 0032534754 scopus 로고    scopus 로고
    • The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure of a putative ABC-type binding protein
    • Lawrence M.C., Pilling P.A., Epa V.C., Berry A.M., Ogunniyi A.D., Paton J.C. The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure of 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
  • 15
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho F.A., Ledvina P.S. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 20:1996;17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 16
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost B. PHD: predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol. 266:1996;525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 17
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., 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
  • 18
    • 0029032964 scopus 로고
    • MolView: A program to analyze and display atomic structures on the Macintosh personal computer
    • Smith T.J. MolView: a program to analyze and display atomic structures on the Macintosh personal computer. J. Mol. Graph. 13:1995;122-125.
    • (1995) J. Mol. Graph. , vol.13 , pp. 122-125
    • Smith, T.J.1
  • 19
    • 0031081208 scopus 로고    scopus 로고
    • The adc locus, which affects competence for genetic transformation in Streptococcus pneumoniae, encodes an ABC transporter with a putative lipoprotein homologous to a family of streptococcal adhesins
    • Dintilhac A., Claverys J.P. The adc locus, which affects competence for genetic transformation in Streptococcus pneumoniae, encodes an ABC transporter with a putative lipoprotein homologous to a family of streptococcal adhesins. Res. Microbiol. 148:1997;119-131.
    • (1997) Res. Microbiol. , vol.148 , pp. 119-131
    • Dintilhac, A.1    Claverys, J.P.2
  • 21
    • 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
  • 22
    • 0033137141 scopus 로고    scopus 로고
    • The Irt1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range
    • Korshunova Y.O., Eide D., Clark W.G., Guerinot M.L., Pakrasi H.B. The Irt1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range. Plant Mol. Biol. 40:1999;37-44.
    • (1999) Plant Mol. Biol. , vol.40 , pp. 37-44
    • Korshunova, Y.O.1    Eide, D.2    Clark, W.G.3    Guerinot, M.L.4    Pakrasi, H.B.5
  • 23
    • 0036431502 scopus 로고    scopus 로고
    • A new zinc-protein coordination site in intracellular metal trafficking: Solution structure of the Apo and Zn(II) forms of ZntA(46-118)
    • Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E., O'Halloran T.V. A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118). J. Mol. Biol. 323:2002;883-897.
    • (2002) J. Mol. Biol. , vol.323 , pp. 883-897
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Finney, L.A.4    Outten, C.E.5    O'Halloran, T.V.6
  • 24
    • 0042208193 scopus 로고    scopus 로고
    • The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate
    • Hou Z., Mitra B. The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate. J. Biol. Chem. 278:2003;2845-2846.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2845-2846
    • Hou, Z.1    Mitra, B.2
  • 25
    • 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
    • Mitra A., Sharma R. 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, A.1    Sharma, R.2
  • 26
    • 1342344814 scopus 로고    scopus 로고
    • The SLC39 family of metal ion transporters
    • Online First. doi: 10.1007/s00424-003-1074-3
    • Eide D.J. The SLC39 family of metal ion transporters. Pflugers Arch. 2003;. Online First. doi: 10.1007/s00424-003-1074-3.
    • (2003) Pflugers Arch.
    • Eide, D.J.1
  • 27
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallog. sect. D. 57:2001;1373-1382.
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 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
  • 32
    • 0002700643 scopus 로고
    • Halloween...masks and bones
    • S. Bailey, R. Hubbard, & D. Waller. Daresbury, UK: SERC Daresbury Laboratory
    • Kleywegt G.J., Jones T.A. Halloween...masks and bones. Bailey S., Hubbard R., Waller D. From First Map to Final Model. 1994;59-66 SERC Daresbury Laboratory, Daresbury, UK.
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 33
    • 0033119386 scopus 로고    scopus 로고
    • Software for handling macromolecular envelopes
    • Kleywegt G.J., Jones T.A. Software for handling macromolecular envelopes. Acta Crystallog. sect. D. 55:1999;941-944.
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 941-944
    • Kleywegt, G.J.1    Jones, T.A.2
  • 34
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 36
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 37
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.