TY - JOUR
T1 - Structure of AmpC β-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix
AU - Yamaguchi, Yoshihiro
AU - Sato, Genta
AU - Yamagata, Yuriko
AU - Doi, Yohei
AU - Wachino, Jun Ichi
AU - Arakawa, Yoshichika
AU - Matsuda, Koki
AU - Kurosaki, Hiromasa
PY - 2009
Y1 - 2009
N2 - The X-ray crystal structure of AmpC β-lactamase (AmpCD) with a tripeptide deletion (Gly286-Ser287-Asp288) produced by Escherichia coli HKY28, a ceftazidime-resistant strain, was determined at a resolution of 1.7 Å. The structure of AmpCD 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 -helix present in the native AmpC β-lactamase of E. coli to a loop structure, which results in a widening of the substrate-binding site.
AB - The X-ray crystal structure of AmpC β-lactamase (AmpCD) with a tripeptide deletion (Gly286-Ser287-Asp288) produced by Escherichia coli HKY28, a ceftazidime-resistant strain, was determined at a resolution of 1.7 Å. The structure of AmpCD 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 -helix present in the native AmpC β-lactamase of E. coli to a loop structure, which results in a widening of the substrate-binding site.
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U2 - 10.1107/S1744309109014249
DO - 10.1107/S1744309109014249
M3 - Article
C2 - 19478427
AN - SCOPUS:67649130236
SN - 1744-3091
VL - 65
SP - 540
EP - 543
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 6
ER -