메뉴 건너뛰기




Volumn 49, Issue 25, 2010, Pages 5206-5212

The 1.4 Å crystal structure of the arsd arsenic metallochaperone provides insights into its interaction with the ArsA ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ASYMMETRIC UNIT; BACTERIAL RESISTANCE; CATALYTIC SUBUNITS; DOCKING MODELS; HAZARDOUS CHEMICALS; STRUCTURAL MODELS; SULFUR ATOMS; THIOREDOXIN-FOLD;

EID: 77953902537     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100571r     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0037656482 scopus 로고    scopus 로고
    • Health effects and risk assessment of arsenic
    • Abernathy, C. O., Thomas, D. J., and Calderon, R. L. (2003) Health effects and risk assessment of arsenic J. Nutr. 133, 1536S-1538S
    • (2003) J. Nutr. , vol.133
    • Abernathy, C.O.1    Thomas, D.J.2    Calderon, R.L.3
  • 3
    • 36348997984 scopus 로고    scopus 로고
    • Arsenic metabolism in prokaryotic and eukaryotic microbes
    • (Nies, D. H. S. and Simon, Eds.) Springer-Verlag, Heidelberg/New York
    • Bhattacharjee, H. and Rosen, B. P. (2007) Arsenic metabolism in prokaryotic and eukaryotic microbes, in Molecular microbiology of heavy metals (Nies, D. H. S. and Simon, Eds.) pp 371 - 406, Springer-Verlag, Heidelberg/New York.
    • (2007) Molecular Microbiology of Heavy Metals , pp. 371-406
    • Bhattacharjee, H.1    Rosen, B.P.2    Nies, D.H.S.3
  • 4
    • 33750371052 scopus 로고    scopus 로고
    • An arsenic metallochaperone for an arsenic detoxification pump
    • Lin, Y. F., Walmsley, A. R., and Rosen, B. P. (2006) An arsenic metallochaperone for an arsenic detoxification pump Proc. Natl. Acad. Sci. U.S.A. 103, 15617-15622
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15617-15622
    • Lin, Y.F.1    Walmsley, A.R.2    Rosen, B.P.3
  • 5
    • 34447116980 scopus 로고    scopus 로고
    • ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity
    • Lin, Y. F., Yang, J., and Rosen, B. P. (2007) ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity J. Biol. Chem. 282, 16783-16791
    • (2007) J. Biol. Chem. , vol.282 , pp. 16783-16791
    • Lin, Y.F.1    Yang, J.2    Rosen, B.P.3
  • 6
    • 77951679239 scopus 로고    scopus 로고
    • Arsenic binding and transfer by the ArsD As(III) metallochaperone
    • Yang, J., Rawat, S., Stemmler, T. L., and Rosen, B. P. (2010) Arsenic binding and transfer by the ArsD As(III) metallochaperone. Biochemistry 49, 3658 - 3666.
    • (2010) Biochemistry , vol.49 , pp. 3658-3666
    • Yang, J.1    Rawat, S.2    Stemmler, T.L.3    Rosen, B.P.4
  • 7
    • 37349131627 scopus 로고    scopus 로고
    • Characterization of the metalloactivation domain of an arsenite/antimonite resistance pump
    • Ruan, X., Bhattacharjee, H., and Rosen, B. P. (2008) Characterization of the metalloactivation domain of an arsenite/antimonite resistance pump Mol. Microbiol. 67, 392-402
    • (2008) Mol. Microbiol. , vol.67 , pp. 392-402
    • Ruan, X.1    Bhattacharjee, H.2    Rosen, B.P.3
  • 8
    • 70350627430 scopus 로고    scopus 로고
    • Structural biology of copper trafficking
    • Boal, A. K. and Rosenzweig, A. C. (2009) Structural biology of copper trafficking Chem. Rev. 109, 4760-4779
    • (2009) Chem. Rev. , vol.109 , pp. 4760-4779
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 9
    • 38349186555 scopus 로고    scopus 로고
    • ArsD: An As(III) metallochaperone for the ArsAB As(III)-translocating ATPase
    • Lin, Y. F., Yang, J., and Rosen, B. P. (2007) ArsD: an As(III) metallochaperone for the ArsAB As(III)-translocating ATPase J. Bioenerg. Biomembr. 39, 453-458
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 453-458
    • Lin, Y.F.1    Yang, J.2    Rosen, B.P.3
  • 12
    • 0033772589 scopus 로고    scopus 로고
    • Advances in multiple wavelength anomalous diffraction crystallography
    • Ealick, S. E. (2000) Advances in multiple wavelength anomalous diffraction crystallography Curr. Opin. Chem. Biol. 4, 495-499
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 495-499
    • Ealick, S.E.1
  • 14
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn, M. D., Murshudov, G. N., and Papiz, M. Z. (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions Methods Enzymol. 374, 300-321
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 17
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8, 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 18
    • 0030917793 scopus 로고    scopus 로고
    • Metalloregulatory properties of the ArsD repressor
    • Chen, Y. and Rosen, B. P. (1997) Metalloregulatory properties of the ArsD repressor J. Biol. Chem. 272, 14257-14262
    • (1997) J. Biol. Chem. , vol.272 , pp. 14257-14262
    • Chen, Y.1    Rosen, B.P.2
  • 20
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm, L., Kaariainen, S., Rosenstrom, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3 Bioinformatics 24, 2780-2781
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 21
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti, S. K., LeMaster, D. M., and Eklund, H. (1990) Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution J. Mol. Biol. 212, 167-184
    • (1990) J. Mol. Biol. , vol.212 , pp. 167-184
    • Katti, S.K.1    Lemaster, D.M.2    Eklund, H.3
  • 22
    • 22244473019 scopus 로고    scopus 로고
    • The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant
    • Collet, J. F., Peisach, D., Bardwell, J. C., and Xu, Z. (2005) The crystal structure of TrxA(CACA): insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant Protein Sci. 14, 1863-1869
    • (2005) Protein Sci. , vol.14 , pp. 1863-1869
    • Collet, J.F.1    Peisach, D.2    Bardwell, J.C.3    Xu, Z.4
  • 23
    • 33744508953 scopus 로고    scopus 로고
    • Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase
    • Ruan, X., Bhattacharjee, H., and Rosen, B. P. (2006) Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase J. Biol. Chem. 281, 9925-9934
    • (2006) J. Biol. Chem. , vol.281 , pp. 9925-9934
    • Ruan, X.1    Bhattacharjee, H.2    Rosen, B.P.3
  • 24
    • 0034282542 scopus 로고    scopus 로고
    • Structure of the ArsA ATPase: The catalytic subunit of a heavy metal resistance pump
    • Zhou, T., Radaev, S., Rosen, B. P., and Gatti, D. L. (2000) Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump EMBO J. 19, 1-8
    • (2000) EMBO J. , vol.19 , pp. 1-8
    • Zhou, T.1    Radaev, S.2    Rosen, B.P.3    Gatti, D.L.4
  • 25
    • 0035839434 scopus 로고    scopus 로고
    • Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation
    • Zhou, T., Radaev, S., Rosen, B. P., and Gatti, D. L. (2001) Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation J. Biol. Chem. 276, 30414-30422
    • (2001) J. Biol. Chem. , vol.276 , pp. 30414-30422
    • Zhou, T.1    Radaev, S.2    Rosen, B.P.3    Gatti, D.L.4
  • 26
    • 0037412034 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance
    • Shen, J., Hsu, C. M., Kang, B. K., Rosen, B. P., and Bhattacharjee, H. (2003) The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance Biometals 16, 369-378
    • (2003) Biometals , vol.16 , pp. 369-378
    • Shen, J.1    Hsu, C.M.2    Kang, B.K.3    Rosen, B.P.4    Bhattacharjee, H.5
  • 27
    • 33748901612 scopus 로고    scopus 로고
    • The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae
    • Auld, K. L., Hitchcock, A. L., Doherty, H. K., Frietze, S., Huang, L. S., and Silver, P. A. (2006) The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae Genetics 174, 215-227
    • (2006) Genetics , vol.174 , pp. 215-227
    • Auld, K.L.1    Hitchcock, A.L.2    Doherty, H.K.3    Frietze, S.4    Huang, L.S.5    Silver, P.A.6
  • 30
    • 0035986679 scopus 로고    scopus 로고
    • Metallochaperones: Bind and deliver
    • Rosenzweig, A. C. (2002) Metallochaperones: bind and deliver Chem. Biol. 9, 673-677
    • (2002) Chem. Biol. , vol.9 , pp. 673-677
    • Rosenzweig, A.C.1
  • 32
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb, A. L., Torres, A. S., OHalloran, T. V., and Rosenzweig, A. C. (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone Nat. Struct. Biol. 8, 751-755
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    Ohalloran, T.V.3    Rosenzweig, A.C.4
  • 33
    • 1842450290 scopus 로고    scopus 로고
    • A docking approach to the study of copper trafficking proteins; Interaction between metallochaperones and soluble domains of copper ATPases
    • Arnesano, F., Banci, L., Bertini, I., and Bonvin, A. M. (2004) A docking approach to the study of copper trafficking proteins; interaction between metallochaperones and soluble domains of copper ATPases Structure 12, 669-676
    • (2004) Structure , vol.12 , pp. 669-676
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Bonvin, A.M.4
  • 34
    • 0030795417 scopus 로고    scopus 로고
    • Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase
    • Zhou, T. and Rosen, B. P. (1997) Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase J. Biol. Chem. 272, 19731-19737
    • (1997) J. Biol. Chem. , vol.272 , pp. 19731-19737
    • Zhou, T.1    Rosen, B.P.2
  • 35
    • 0033119231 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773
    • Zhou, T., Rosen, B. P., and Gatti, D. L. (1999) Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773 Acta Crystallogr., Sect. D: Biol. Crystallogr. 55, 921-924
    • (1999) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.55 , pp. 921-924
    • Zhou, T.1    Rosen, B.P.2    Gatti, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.