메뉴 건너뛰기




Volumn 6, Issue 12, 1997, Pages 2671-2676

Crystal structures of the cadmium- and mercury-substituted metallo-β- lactamase from Bacteroides fragilis

Author keywords

Binuclear metal center; Cadmium binding; Mercury binding; Metallo lactamase; X ray structure

Indexed keywords

BACTERIAL ENZYME; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CADMIUM; CYSTEINE; MERCURY; METALLOPROTEIN; ZINC;

EID: 0031440226     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061225     Document Type: Article
Times cited : (57)

References (19)
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger AT. 1992b. Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 6
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi A, Pares S, Duée E, Galleni M, Duez C, Frère JM, Dideherg O. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 14:4919-4921.
    • (1995) EMBO J , vol.14 , pp. 4919-4921
    • Carfi, A.1    Pares, S.2    Duée, E.3    Galleni, M.4    Duez, C.5    Frère, J.M.6    Dideherg, O.7
  • 7
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
    • Concha NO, Rasmussen BA, Bush K, Herzberg O. 1996. Crystal structure of the wide-spectrum binuclear zinc β-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
  • 8
    • 0029808391 scopus 로고    scopus 로고
    • Characterization of the metal-binding sites of the β-lactamase from Bacteroides fragilis
    • Crowder MW, Wang Z, Franklin SL, Zovinka EP, Benkovic SJ. 1996. Characterization of the metal-binding sites of the β-lactamase from Bacteroides fragilis. Biochemistry 35:12126-12132.
    • (1996) Biochemistry , vol.35 , pp. 12126-12132
    • Crowder, M.W.1    Wang, Z.2    Franklin, S.L.3    Zovinka, E.P.4    Benkovic, S.J.5
  • 9
    • 0016302079 scopus 로고
    • Metal cofactor requirements of β-lactamase II
    • Davies RB, Abraham EP. 1974. Metal cofactor requirements of β-lactamase II. Biochem J 143: 129-135.
    • (1974) Biochem J , vol.143 , pp. 129-135
    • Davies, R.B.1    Abraham, E.P.2
  • 10
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. 1991. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A 47:392-400.
    • (1991) Acta Crystallogr A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 12
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. 1988. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J Appl Crystallogr 21:916-924.
    • (1988) J Appl Crystallogr , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 13
    • 85027633237 scopus 로고
    • Crystal orientation and X-ray pattern prediction routines for area detector diffractometer systems in macromolecular crystallography
    • Messerschmidt A, Pflugrath JW. 1987. Crystal orientation and X-ray pattern prediction routines for area detector diffractometer systems in macromolecular crystallography. J Appl Crystallogr 20:306-315.
    • (1987) J Appl Crystallogr , vol.20 , pp. 306-315
    • Messerschmidt, A.1    Pflugrath, J.W.2
  • 14
    • 0027284501 scopus 로고
    • Metallo-β-lactamases - A new therapeutic challenge
    • Payne DJ. 1993. Metallo-β-lactamases - A new therapeutic challenge. J Med Microbiol 39:93-99.
    • (1993) J Med Microbiol , vol.39 , pp. 93-99
    • Payne, D.J.1
  • 16
    • 0027958918 scopus 로고
    • Contribution of enzymatic properties, cell permeability, and enzyme expression to microbiological activities of β-lactams in three Bacteroides fragilis isolates that harbor a metallo-β-lactamase gene
    • Rasmussen BA, Yang Y, Jacobus N, Bush K. 1994. Contribution of enzymatic properties, cell permeability, and enzyme expression to microbiological activities of β-lactams in three Bacteroides fragilis isolates that harbor a metallo-β-lactamase gene. Antimicrob Agents Chemother 38:2116-2120.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 2116-2120
    • Rasmussen, B.A.1    Yang, Y.2    Jacobus, N.3    Bush, K.4
  • 17
    • 0013865825 scopus 로고
    • Zinc as cofactor for cephalosporinase from Bacillus cereus 569
    • Sabath LD, Abraham EP. 1966. Zinc as cofactor for cephalosporinase from Bacillus cereus 569. Biochem J 98:11c-13c.
    • (1966) Biochem J , vol.98
    • Sabath, L.D.1    Abraham, E.P.2
  • 19
    • 0026651129 scopus 로고
    • Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636
    • Yang Y, Rasmussen BA, Bush K. 1992. Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636. Antimicrob Agents Chemother 36:1155-1157.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 1155-1157
    • Yang, Y.1    Rasmussen, B.A.2    Bush, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.