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

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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.

Original languageEnglish
Pages (from-to)540-543
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number6
Publication statusPublished - 10-07-2009
Externally publishedYes


All Science Journal Classification (ASJC) codes

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

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