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

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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
Volume65
Issue number6
DOIs
Publication statusPublished - 10-07-2009
Externally publishedYes

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deletion
Escherichia
helices
Escherichia coli
Ceftazidime
Crystal structure
Binding Sites
X-Rays
X rays
crystal structure
causes
Substrates
x rays

All Science Journal Classification (ASJC) codes

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

Cite this

Yamaguchi, Yoshihiro ; Sato, Genta ; Yamagata, Yuriko ; Doi, Yohei ; Wachino, Jun Ichi ; Arakawa, Yoshichika ; Matsuda, Koki ; Kurosaki, Hiromasa. / Structure of AmpC β-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2009 ; Vol. 65, No. 6. pp. 540-543.
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abstract = "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 {\AA}. 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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Structure of AmpC β-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix. / Yamaguchi, Yoshihiro; Sato, Genta; Yamagata, Yuriko; Doi, Yohei; Wachino, Jun Ichi; Arakawa, Yoshichika; Matsuda, Koki; Kurosaki, Hiromasa.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 6, 10.07.2009, p. 540-543.

Research output: Contribution to journalArticle

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AU - Matsuda, Koki

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