메뉴 건너뛰기




Volumn 73, Issue 4, 2008, Pages 1053-1057

Crystal structure of TTHA1429, a novel metallo-β-lactamase superfamily protein from Thermus thermophilus HB8

Author keywords

Crystal structure; Hydrolase; Metallo beta lactamase; Thermus thermophilus; Zinc

Indexed keywords

METALLO BETA LACTAMASE; PROTEIN TTHA1429; UNCLASSIFIED DRUG; BETA LACTAMASE; METAL;

EID: 58149277687     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22215     Document Type: Article
Times cited : (6)

References (19)
  • 1
    • 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, Dideberg O. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 1995;14:4914-4921.
    • (1995) EMBO J , vol.14 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duée, E.3    Galleni, M.4    Duez, C.5    Frère, J.M.6    Dideberg, O.7
  • 2
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β- Lactamase from Bacteroides fragilis
    • DOI 10.1016/S0969-2126(96)00089-5
    • Concha NO, Rasmussen BA, Bush K, Herzberg O. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 1996;4:823-836. (Pubitemid 26312366)
    • (1996) Structure , vol.4 , Issue.7 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 3
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • DOI 10.1016/j.bcp.2007.05.021, PII S0006295207003309
    • Bebrone C. Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem Pharmacol 2007;74:1686-1701. (Pubitemid 350088675)
    • (2007) Biochemical Pharmacology , vol.74 , Issue.12 , pp. 1686-1701
    • Bebrone, C.1
  • 4
    • 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. Processing of X-ray diffraction collected in oscillation mode. Methods Enzymol 1997;276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:7600-7603.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 7600-7603
  • 11
  • 12
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968; 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 14
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C. Dali: a network tool for protein structure comparison. Trends Biochem Sci 1995;20:478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 16
    • 0032510815 scopus 로고    scopus 로고
    • Unanticipated inhibition of the metallo-β-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): A crystallographic study at 1.85-Å Resolution
    • DOI 10.1021/bi9730339
    • Fitzgerald PM, Wu JK, Toney JH. Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-Å resolution. Biochemistry 1998;37:6791-6800. (Pubitemid 28228114)
    • (1998) Biochemistry , vol.37 , Issue.19 , pp. 6791-6800
    • Fitzgerald, P.M.D.1    Wu, J.K.2    Toney, J.H.3
  • 18
    • 33644948482 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-beta-lactamases
    • Murphy TA, Catto LE, Halford SE, Hadfield AT, Minor W, Walsh TR, Spencer J. Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-beta-lactamases. J Mol Biol 2006;357:890-903.
    • (2006) J Mol Biol , vol.357 , pp. 890-903
    • Murphy, T.A.1    Catto, L.E.2    Halford, S.E.3    Hadfield, A.T.4    Minor, W.5    Walsh, T.R.6    Spencer, J.7
  • 19
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J. DaliLite workbench for protein structure comparison. Bioinformatics 2000;16:566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.