Structure of AmpC beta-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix.
The X-ray crystal structure of AmpC beta-lactamase (AmpC(D)) with a tripeptide deletion (Gly286-Ser287-Asp288) produced by Escherichia coli HKY28, a ceftazidime-resistant strain, was determined at a resolution of 1.7 A. The structure of AmpC(D) suggests that the tripeptide deletion at positions 286-288 located in the H10 helix causes a structural change of the Asn289-Asn294 region from the alpha-helix present in the native AmpC beta-lactamase of E. coli to a loop structure, which results in a widening of the substrate-binding site.
Yamaguchi
Yoshihiro
Y
Environmental Safety Center, Kumamoto University, Kumamoto, Japan. yyamagu@gpo.kumamoto-u.ac.jp
Sato
Genta
G
Yamagata
Yuriko
Y
Doi
Yohei
Y
Wachino
Jun-ichi
J
Arakawa
Yoshichika
Y
Matsuda
Koki
K
Kurosaki
Hiromasa
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D001665:Binding Sites / Q000235:genetics; D018360:Crystallography, X-Ray; D003625:Data Collection; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017384:Sequence Deletion; D055672:Static Electricity; D013223:Statistics as Topic; D013379:Substrate Specificity; D014867:Water / Q000737:chemistry; D001618:beta-Lactamases / Q000737:chemistry* / Q000235:genetics*
D001426:Bacterial Proteins; D014867:Water; C048795:AmpC beta-lactamases; D001618:beta-Lactamases