Structure of AmpC β-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 65, Issue 6, 2009, Pages 540-543

  Yamaguchi, Yoshihiro ^a   Sato, Genta ^a   Yamagata, Yuriko ^a   Doi, Yohei ^b   Wachino, Jun Ichi ^b   Arakawa, Yoshichika ^b   Matsuda, Koki ^a   Kurosaki, Hiromasa ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

Author keywords

lactam antibiotics; AmpC lactamase

Indexed keywords

ESCHERICHIA COLI;

AMPC BETA LACTAMASES; AMPC BETA-LACTAMASES; BACTERIAL PROTEIN; BETA LACTAMASE; WATER;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENE DELETION; GENETICS; HUMAN; HYDROGEN BOND; INFORMATION PROCESSING; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; STATIC ELECTRICITY; STATISTICS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BETA-LACTAMASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DATA COLLECTION; ESCHERICHIA COLI; HUMANS; HYDROGEN BONDING; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE DELETION; STATIC ELECTRICITY; STATISTICS AS TOPIC; SUBSTRATE SPECIFICITY; WATER;

EID: 67649130236     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309109014249     Document Type: Article

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