Crystal structure of the extended-spectrum β-lactamase PER-2 and insights into the role of specific residues in the interaction with β-lactams and β-lactamase inhibitors

Antimicrobial Agents and Chemotherapy

Volumn 58, Issue 10, 2014, Pages 5994-6002

  Ruggiero, Melina ^a   Kerff, Frédéric ^b   Herman, Raphaël ^b   Sapunaric, Frédéric ^b   Galleni, Moreno ^b   Gutkind, Gabriel ^a   Charlier, Paulette ^b   Sauvage, Eric ^b   Power, Pablo ^a  

^a UNIVERSIDAD DE BUENOS AIRES   (Argentina)

^b UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BETA LACTAM; BETA LACTAMASE INHIBITOR; EXTENDED SPECTRUM BETA LACTAMASE; EXTENDED SPECTRUM BETA LACTAMASE PER2; GLUTAMINE; LYSINE; SERINE; THREONINE; UNCLASSIFIED DRUG; WATER; BETA LACTAMASE; CEPHALOSPORIN DERIVATIVE; PROTEIN BINDING;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; NONHUMAN; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROCEDURES; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BETA-LACTAMASE INHIBITORS; BETA-LACTAMASES; BETA-LACTAMS; CEPHALOSPORINS; CRYSTALLOGRAPHY, X-RAY; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84907259455     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00089-14     Document Type: Article

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