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Volumn 275, Issue 36, 2000, Pages 28075-28082

The high resolution crystal structure for class A β-lactamase PER-1 reveals the bases for its increase in breadth of activity

(6) Tranier, Samuel a Bouthors, Anne Typhaine b Maveyraud, Laurent a Guillet, Valérie a Sougakoff, Wladimir b Samama, Jean Pierre a

a INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE (France)

b PITIÉ SALPÊTRIÈRE HOSPITAL (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA LACTAMASE; CEPHALOSPORINASE; PENICILLINASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ESCHERICHIA COLI; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STEREOCHEMISTRY;

AMINO ACID SEQUENCE; BETA-LACTAMASES; CEPHALOSPORINASE; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034623247 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M003802200 Document Type: Article

Times cited : (65)

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