메뉴 건너뛰기




Volumn 50, Issue 2, 2006, Pages 215-222

The molybdate-binding protein (ModA) of the plant pathogen Xanthomonas axonopodis pv. citri

Author keywords

ABC transporters; ModA; Molybdate; Molybdate binding protein; Xanthomonas axonopodis pv. citri

Indexed keywords

ABC TRANSPORTER; BACTERIAL PROTEIN; MOLYBDENUM; MOLYBDIC ACID; PERIPLASMIC BINDING PROTEIN; RECOMBINANT PROTEIN; TUNGSTEN DERIVATIVE; TUNGSTIC ACID;

EID: 33750826498     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.06.014     Document Type: Article
Times cited : (19)

References (38)
  • 2
    • 0036363905 scopus 로고    scopus 로고
    • Transport, homeostasis, regulation, and binding of molybdate and tungstate to proteins
    • Pau R.N., and Lawson D.M. Transport, homeostasis, regulation, and binding of molybdate and tungstate to proteins. Met. Ions Biol. Syst. 39 (2002) 31-74
    • (2002) Met. Ions Biol. Syst. , vol.39 , pp. 31-74
    • Pau, R.N.1    Lawson, D.M.2
  • 3
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • Rajagopalan K.V., and Johnson J.L. The pterin molybdenum cofactors. J. Biol. Chem. 267 (1992) 10199-10202
    • (1992) J. Biol. Chem. , vol.267 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 4
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor-containing enzymes: Structure and Mechanism
    • Kisker C., Schindelin H., and Rees D.C. Molybdenum-cofactor-containing enzymes: Structure and Mechanism. Ann. Rev. Biochem. 66 (1997) 233-267
    • (1997) Ann. Rev. Biochem. , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 6
    • 0030726129 scopus 로고    scopus 로고
    • Molybdate transport and regulation in bacteria
    • Grunden A.M., and Shanmugam K.T. Molybdate transport and regulation in bacteria. Arch. Microbiol. 168 (1997) 345-354
    • (1997) Arch. Microbiol. , vol.168 , pp. 345-354
    • Grunden, A.M.1    Shanmugam, K.T.2
  • 8
    • 0023272628 scopus 로고
    • Cloning and nucleotide sequence of the chlD locus
    • Johann S., and Hinton S.M. Cloning and nucleotide sequence of the chlD locus. J. Bacteriol. 169 (1987) 1911-1916
    • (1987) J. Bacteriol. , vol.169 , pp. 1911-1916
    • Johann, S.1    Hinton, S.M.2
  • 9
    • 0028851284 scopus 로고
    • Regulation of the molybdate transport operon, modABCD, of Escherichia coli in response to molybdate availability
    • Rech S., Deppenmeier U., and Gunsalus R.P. Regulation of the molybdate transport operon, modABCD, of Escherichia coli in response to molybdate availability. J. Bacteriol. 177 (1995) 1023-1029
    • (1995) J. Bacteriol. , vol.177 , pp. 1023-1029
    • Rech, S.1    Deppenmeier, U.2    Gunsalus, R.P.3
  • 11
    • 0030023719 scopus 로고    scopus 로고
    • Properties of the Periplasmic ModA Molybdate-binding protein of Escherichia coli
    • Rech S., Wolin C., and Gunsalus R.P. Properties of the Periplasmic ModA Molybdate-binding protein of Escherichia coli. J. Biol. Chem. 271 (1996) 2557-2562
    • (1996) J. Biol. Chem. , vol.271 , pp. 2557-2562
    • Rech, S.1    Wolin, C.2    Gunsalus, R.P.3
  • 13
    • 0033588028 scopus 로고    scopus 로고
    • An analysis of the binding of repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli
    • Grunden A.M., Self W.T., Villain M., Blalock J.E., and Shanmugam K.T. An analysis of the binding of repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli. J. Biol. Chem. 274 (1999) 24308-24315
    • (1999) J. Biol. Chem. , vol.274 , pp. 24308-24315
    • Grunden, A.M.1    Self, W.T.2    Villain, M.3    Blalock, J.E.4    Shanmugam, K.T.5
  • 14
    • 0027467467 scopus 로고
    • Characterization of genes involved in molybdenium transport in Azotobacter vinelandi
    • Luque F., Mitchenall L.A., Chapman M., Cristine R., and Pau R.N. Characterization of genes involved in molybdenium transport in Azotobacter vinelandi. Mol. Microbiol. 7 (1993) 457-459
    • (1993) Mol. Microbiol. , vol.7 , pp. 457-459
    • Luque, F.1    Mitchenall, L.A.2    Chapman, M.3    Cristine, R.4    Pau, R.N.5
  • 15
    • 0032804540 scopus 로고    scopus 로고
    • Characterization of the molybdate transport system ModABC of Staphylococus carnosus
    • Neubauer H., Pantel I., Lindgren P.E., and Gotz F. Characterization of the molybdate transport system ModABC of Staphylococus carnosus. Arch. Microbiol. 172 (1999) 109-115
    • (1999) Arch. Microbiol. , vol.172 , pp. 109-115
    • Neubauer, H.1    Pantel, I.2    Lindgren, P.E.3    Gotz, F.4
  • 16
    • 0027175827 scopus 로고
    • Characterization of the Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenum-pterin-binding proteins
    • Wang G., Angermuller S., and Klipp W. Characterization of the Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenum-pterin-binding proteins. J. Bacteriol. 175 (1993) 3031-3042
    • (1993) J. Bacteriol. , vol.175 , pp. 3031-3042
    • Wang, G.1    Angermuller, S.2    Klipp, W.3
  • 17
    • 0037213708 scopus 로고    scopus 로고
    • Transport of molybdate in the cyanobacterium Anabaena variabilis ATCC 29413
    • Thiel T., Pratte B., and Zabalak M. Transport of molybdate in the cyanobacterium Anabaena variabilis ATCC 29413. Arch. Microbiol. 179 (2002) 50-56
    • (2002) Arch. Microbiol. , vol.179 , pp. 50-56
    • Thiel, T.1    Pratte, B.2    Zabalak, M.3
  • 18
    • 0942301204 scopus 로고    scopus 로고
    • Molybdate transport and its effect on nitrogen utilization in the cyanobacterium Anabaena variabilis ATCC 29419
    • Zahalak M., Pratte B., Werth K.J., and Thiel T. Molybdate transport and its effect on nitrogen utilization in the cyanobacterium Anabaena variabilis ATCC 29419. Mol. Microbiol. 51 (2004) 539-549
    • (2004) Mol. Microbiol. , vol.51 , pp. 539-549
    • Zahalak, M.1    Pratte, B.2    Werth, K.J.3    Thiel, T.4
  • 19
    • 30744477218 scopus 로고    scopus 로고
    • Functional characterization of the Bradyrizobium japonicum modA and modB genes involved in molybdenum transport
    • Delgado M.J., Tresierra-Ayala A., Talbi C., and Bedmar E.J. Functional characterization of the Bradyrizobium japonicum modA and modB genes involved in molybdenum transport. Microbiology 152 (2006) 199-207
    • (2006) Microbiology , vol.152 , pp. 199-207
    • Delgado, M.J.1    Tresierra-Ayala, A.2    Talbi, C.3    Bedmar, E.J.4
  • 20
    • 0031228463 scopus 로고    scopus 로고
    • Crystal structure of molybdate-binding protein ModA
    • Hu Y., Rech S., Gunsalus R.P., and Rees D.C. Crystal structure of molybdate-binding protein ModA. Nat. Struct. Biol. 4 (1997) 703-707
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 703-707
    • Hu, Y.1    Rech, S.2    Gunsalus, R.P.3    Rees, D.C.4
  • 21
    • 33748507351 scopus 로고    scopus 로고
    • Proteins ligand for molybdate, specificity and charge stabilization at the anion-binding sites of periplasmic and intracellular molybdate-binding proteins of Azotobacter vinelandii
    • Lawson D.M., Williams C.E., White D.J., Choay A.P., Mitchenall L.A., and Pau R.N. Proteins ligand for molybdate, specificity and charge stabilization at the anion-binding sites of periplasmic and intracellular molybdate-binding proteins of Azotobacter vinelandii. J. Chem. Soc., Dalton Trans. 21 (1997) 3981-3984
    • (1997) J. Chem. Soc., Dalton Trans. , vol.21 , pp. 3981-3984
    • Lawson, D.M.1    Williams, C.E.2    White, D.J.3    Choay, A.P.4    Mitchenall, L.A.5    Pau, R.N.6
  • 22
    • 0032534765 scopus 로고    scopus 로고
    • Ligand-size is the major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 Å resolution crystal structure of Azotobacter vinelandii ModA
    • Lawson D.M., Williams C.E., Mitchenall L.A., and Pau R.N. Ligand-size is the major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 Å resolution crystal structure of Azotobacter vinelandii ModA. Struct. Fold. Des. 6 (1998) 1529-1539
    • (1998) Struct. Fold. Des. , vol.6 , pp. 1529-1539
    • Lawson, D.M.1    Williams, C.E.2    Mitchenall, L.A.3    Pau, R.N.4
  • 23
    • 0037681624 scopus 로고    scopus 로고
    • Xanthomonas citri: breaking the surface
    • Brunings A.M., and Gabriel D.W. Xanthomonas citri: breaking the surface. Mol. Plant Pathol. 4 (2003) 141-147
    • (2003) Mol. Plant Pathol. , vol.4 , pp. 141-147
    • Brunings, A.M.1    Gabriel, D.W.2
  • 24
    • 0037161811 scopus 로고    scopus 로고
    • Comparison of the genomes of two Xanthomonas pathogens with differing host specificities
    • da Silva A.C., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., et al. Comparison of the genomes of two Xanthomonas pathogens with differing host specificities. Nature 417 (2002) 459-463
    • (2002) Nature , vol.417 , pp. 459-463
    • da Silva, A.C.1    Ferro, J.A.2    Reinach, F.C.3    Farah, C.S.4    Furlan, L.R.5
  • 25
    • 3242887157 scopus 로고    scopus 로고
    • CD-search: protein domain annotations on the fly
    • Marchler-Bauer A., and Bryant S.H. CD-search: protein domain annotations on the fly. Nucleic Acids Res. 32 (2004) 327-331
    • (2004) Nucleic Acids Res. , vol.32 , pp. 327-331
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 26
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6 (1967) 1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 27
    • 0018374688 scopus 로고
    • A graphical correction procedure for inner filter effect in fluorescence quenching titrations
    • Mertens M.L., and Kägi J.H.R. A graphical correction procedure for inner filter effect in fluorescence quenching titrations. Anal. Biochem. 96 (1979) 448-455
    • (1979) Anal. Biochem. , vol.96 , pp. 448-455
    • Mertens, M.L.1    Kägi, J.H.R.2
  • 30
    • 84990658473 scopus 로고
    • Analysis of X-ray spectra by interative least squares (AXIL): new developments
    • Vekemans B., Janssens K., Vincze L., Adams F., and Vanspen P.E. Analysis of X-ray spectra by interative least squares (AXIL): new developments. X-ray Spectrom. 23 (1994) 278-285
    • (1994) X-ray Spectrom. , vol.23 , pp. 278-285
    • Vekemans, B.1    Janssens, K.2    Vincze, L.3    Adams, F.4    Vanspen, P.E.5
  • 31
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Bohm G., Murh R., and Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5 (1992) 191-195
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Bohm, G.1    Murh, R.2    Jaenicke, R.3
  • 32
  • 33
    • 33645732123 scopus 로고    scopus 로고
    • Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri
    • Santacruz C.P., Balan A., Ferreira L.C.S., and Barbosa J.A. Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. Acta Crystallogr. Sect. F. Struct. Biol. Crystal. Commun. 62 (2006) 289-291
    • (2006) Acta Crystallogr. Sect. F. Struct. Biol. Crystal. Commun. , vol.62 , pp. 289-291
    • Santacruz, C.P.1    Balan, A.2    Ferreira, L.C.S.3    Barbosa, J.A.4
  • 34
    • 0032513256 scopus 로고    scopus 로고
    • Molybdate binding by ModA, the periplasmic component of the Escherichia coli mod molybdate transport system
    • Imperial J., Hadi M., and Amy N.K. Molybdate binding by ModA, the periplasmic component of the Escherichia coli mod molybdate transport system. Biochem. Biophys. Acta 1370 (1998) 337-346
    • (1998) Biochem. Biophys. Acta , vol.1370 , pp. 337-346
    • Imperial, J.1    Hadi, M.2    Amy, N.K.3
  • 36
    • 0030917717 scopus 로고    scopus 로고
    • Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli
    • Anderson L.A., Palmer T., Price N.C., Borneman S., Boxer D.H., and Pau R.N. Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli. Eur. J. Biochem. 246 (1997) 119-126
    • (1997) Eur. J. Biochem. , vol.246 , pp. 119-126
    • Anderson, L.A.1    Palmer, T.2    Price, N.C.3    Borneman, S.4    Boxer, D.H.5    Pau, R.N.6
  • 37
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: a versatile superfamily for protein engineering
    • Dwyer M.A., and Hellinga H. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr. Opin. Struct. Biol. 14 (2004) 495-504
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.2
  • 38
    • 1942486282 scopus 로고    scopus 로고
    • The oligopeptide permease (Opp) of the plant pathogen Xanthomonas axonopodis pv. citri
    • Moutran A., Quaggio R.B., Balan A., Ferreira L.C.S., and Ferreira R.C.C. The oligopeptide permease (Opp) of the plant pathogen Xanthomonas axonopodis pv. citri. Curr. Microbiol. 48 (2004) 354-359
    • (2004) Curr. Microbiol. , vol.48 , pp. 354-359
    • Moutran, A.1    Quaggio, R.B.2    Balan, A.3    Ferreira, L.C.S.4    Ferreira, R.C.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.