메뉴 건너뛰기




Volumn 19, Issue 10, 2010, Pages 1897-1905

Structural and functional characterization of Salmonella enterica serovar typhimurium YcbL: An unusual type II glyoxalase

Author keywords

lactamase; Crystal; Glyoxalase II; Salmonella typhimurium; YcbL; Zinc metallohydrolase

Indexed keywords

FERROUS ION; GLUTATHIONE; GLYOXALASE; UNCLASSIFIED DRUG; YCBL ENZYME;

EID: 77957308830     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.475     Document Type: Article
Times cited : (22)

References (34)
  • 1
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold
    • DOI 10.1016/S0014-5793(01)02686-2, PII S0014579301026862
    • Daiyasu H, Osaka K, Ishino Y, Toh H (2001) Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold. FEBS Lett 503:1-6. (Pubitemid 32769945)
    • (2001) FEBS Letters , vol.503 , Issue.1 , pp. 1-6
    • Daiyasu, H.1    Osaka, K.2    Ishino, Y.3    Toh, H.4
  • 2
    • 3142555854 scopus 로고    scopus 로고
    • Functional and biochemical dissection of the structure-specific nuclease ARTEMIS
    • Pannicke U, Ma Y, Hopfner KP, Niewolik D, Lieber MR, Schwarz K (2004) Functional and biochemical dissection of the structure-specific nuclease ARTEMIS. EMBO J 23:1987-1997.
    • (2004) EMBO J , vol.23 , pp. 1987-1997
    • Pannicke, U.1    Ma, Y.2    Hopfner, K.P.3    Niewolik, D.4    Lieber, M.R.5    Schwarz, K.6
  • 3
    • 23844552796 scopus 로고    scopus 로고
    • Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis
    • Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D (2005) Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proc Natl Acad Sci USA 102:11882-11887.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11882-11887
    • Liu, D.1    Lepore, B.W.2    Petsko, G.A.3    Thomas, P.W.4    Stone, E.M.5    Fast, W.6    Ringe, D.7
  • 5
    • 0032455140 scopus 로고    scopus 로고
    • Quorum sensing and the cell-cell communication dependent regulation of gene expression in pathogenic and non-pathogenic bacteria
    • Hardman AM, Stewart GS, Williams P (1998) Quorum sensing and the cell-cell communication dependent regulation of gene expression in pathogenic and non-pathogenic bacteria. Antonie Van Leeuwenhoek 74:199-210.
    • (1998) Antonie Van Leeuwenhoek , vol.74 , pp. 199-210
    • Hardman, A.M.1    Stewart, G.S.2    Williams, P.3
  • 6
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone C (2007) Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem Pharmacol 74:1686-1701.
    • (2007) Biochem Pharmacol , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 7
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O (1995) The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 14:4914-4921.
    • (1995) EMBO J , vol.14 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duee, E.3    Galleni, M.4    Duez, C.5    Frere, J.M.6    Dideberg, O.7
  • 8
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis
    • Concha NO, Rasmussen BA, Bush K, Herzberg O (1996) Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. Structure 4:823-836.
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 10
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 a resolution
    • Ullah JH, Walsh TR, Taylor IA, Emery DC, Verma CS, Gamblin SJ, Spencer J (1998) The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution. J Mol Biol 284:125-136.
    • (1998) J Mol Biol , vol.284 , pp. 125-136
    • Ullah, J.H.1    Walsh, T.R.2    Taylor, I.A.3    Emery, D.C.4    Verma, C.S.5    Gamblin, S.J.6    Spencer, J.7
  • 11
    • 0035895931 scopus 로고    scopus 로고
    • Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis
    • Zang TM, Hollman DA, Crawford PA, Crowder MW, Makaroff CA (2001) Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis. J Biol Chem 276:4788-4795.
    • (2001) J Biol Chem , vol.276 , pp. 4788-4795
    • Zang, T.M.1    Hollman, D.A.2    Crawford, P.A.3    Crowder, M.W.4    Makaroff, C.A.5
  • 13
    • 0036176228 scopus 로고    scopus 로고
    • Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements
    • DOI 10.1110/ps.31202
    • Gomes CM, Frazao C, Xavier AV, Legall J, Teixeira M (2002) Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements. Protein Sci 11:707-712. (Pubitemid 34171275)
    • (2002) Protein Science , vol.11 , Issue.3 , pp. 707-712
    • Gomes, C.M.1    Frazao, C.2    Xavier, A.V.3    Legall, J.4    Teixeira, M.5
  • 15
    • 34548387498 scopus 로고    scopus 로고
    • Ensemble refinement of protein crystal structures: Validation and application
    • Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN, Jr (2007) Ensemble refinement of protein crystal structures: validation and application. Structure 15:1040-1052.
    • (2007) Structure , vol.15 , pp. 1040-1052
    • Levin, E.J.1    Kondrashov, D.A.2    Wesenberg, G.E.3    Phillips Jr., G.N.4
  • 17
    • 0033200323 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue
    • Cameron AD, Ridderstrom M, Olin B, Mannervik B (1999) Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure 7:1067-1078.
    • (1999) Structure , vol.7 , pp. 1067-1078
    • Cameron, A.D.1    Ridderstrom, M.2    Olin, B.3    Mannervik, B.4
  • 20
    • 34848851672 scopus 로고    scopus 로고
    • Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: New insights into metal ion selectivity
    • Campos-Bermudez VA, Leite NR, Krog R, Costa-Filho AJ, Soncini FC, Oliva G, Vila AJ (2007) Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity. Biochemistry 46:11069-11079.
    • (2007) Biochemistry , vol.46 , pp. 11069-11079
    • Campos-Bermudez, V.A.1    Leite, N.R.2    Krog, R.3    Costa-Filho, A.J.4    Soncini, F.C.5    Oliva, G.6    Vila, A.J.7
  • 23
    • 37849007277 scopus 로고    scopus 로고
    • Catalysis and structural properties of Leishmania infantum glyoxalase II: Trypanothione specificity and phylogeny
    • Silva MS, Barata L, Ferreira AE, Romao S, Tomas AM, Freire AP, Cordeiro C (2008) Catalysis and structural properties of Leishmania infantum glyoxalase II: trypanothione specificity and phylogeny. Biochemistry 47:195-204.
    • (2008) Biochemistry , vol.47 , pp. 195-204
    • Silva, M.S.1    Barata, L.2    Ferreira, A.E.3    Romao, S.4    Tomas, A.M.5    Freire, A.P.6    Cordeiro, C.7
  • 24
    • 33644894229 scopus 로고    scopus 로고
    • Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: Evidence for a novel group of ATP-binding cassette transporters
    • Rodionov DA, Hebbeln P, Gelfand MS, Eitinger T (2006) Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transporters. J Bacteriol 188:317-327.
    • (2006) J Bacteriol , vol.188 , pp. 317-327
    • Rodionov, D.A.1    Hebbeln, P.2    Gelfand, M.S.3    Eitinger, T.4
  • 25
    • 0141928715 scopus 로고    scopus 로고
    • Flexible metal binding of the metallo-beta-lactamase domain: Glyoxalase II incorporates iron, manganese, and zinc in vivo
    • Schilling O, Wenzel N, Naylor M, Vogel A, Crowder M, Makaroff C, Meyer-Klaucke W (2003) Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo. Biochemistry 42:11777-11786.
    • (2003) Biochemistry , vol.42 , pp. 11777-11786
    • Schilling, O.1    Wenzel, N.2    Naylor, M.3    Vogel, A.4    Crowder, M.5    Makaroff, C.6    Meyer-Klaucke, W.7
  • 26
    • 40249091291 scopus 로고    scopus 로고
    • Architectural adaptation and protein expression patterns of Salmonella enterica serovar Enteritidis biofilms under laminar flow conditions
    • Mangalappalli-Illathu AK, Lawrence JR, Swerhone GD, Korber DR (2008) Architectural adaptation and protein expression patterns of Salmonella enterica serovar Enteritidis biofilms under laminar flow conditions. Int J Food Microbiol 123:109-120.
    • (2008) Int J Food Microbiol , vol.123 , pp. 109-120
    • Mangalappalli-Illathu, A.K.1    Lawrence, J.R.2    Swerhone, G.D.3    Korber, D.R.4
  • 27
    • 0020026390 scopus 로고
    • In vitro evaluation of CENTA, a new beta-lactamase-susceptible chromogenic cephalosporin reagent
    • Jones RN, Wilson HW, Novick WJ, Jr, Barry AL, Thornsberry C (1982) In vitro evaluation of CENTA, a new beta-lactamase-susceptible chromogenic cephalosporin reagent. J Clin Microbiol 15:954-958.
    • (1982) J Clin Microbiol , vol.15 , pp. 954-958
    • Jones, R.N.1    Wilson, H.W.2    Novick Jr., W.J.3    Barry, A.L.4    Thornsberry, C.5
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1996) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D Biol Crystallogr D57:122-133.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.D57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 33
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 a
    • Stuart DI, Levine M, Muirhead H, Stammers DK (1979) Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A. J Mol Biol 134:109-142.
    • (1979) J Mol Biol , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.