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

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

研究成果: Article

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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.

元の言語English
ページ(範囲)540-543
ページ数4
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
65
発行部数6
DOI
出版物ステータスPublished - 10-07-2009
外部発表Yes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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