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Volumn 299, Issue 2, 2000, Pages 477-485

The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: Implication in drug resistance

Author keywords

Complex; Drug; Penicillin; Resistance; X ray structure

Indexed keywords

BACTERIAL ENZYME; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CEFUROXIME; GAMMA GLUTAMYLTRANSFERASE; PENICILLIN BINDING PROTEIN; SERINE; THREONINE;

EID: 0034595512     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3740     Document Type: Article
Times cited : (190)

References (43)
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  • 4
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    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 23
    • 0029147002 scopus 로고
    • Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases
    • (1995) Biochemistry , vol.34 , pp. 9532-9540
    • Kuzin, A.P.1    Liu, H.2    Kelly, J.A.3    Knox, J.R.4
  • 25
    • 0025720144 scopus 로고
    • Five independent combinations of mutations can result in low-affinity penicillin-binding protein 2x of Streptococcus pneumoniae
    • (1991) J. Bacteriol. , vol.173 , pp. 6986-6990
    • Laible, G.1    Hakenbeck, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.