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

doi:10.1107/S1744309109014249

Structure of AmpC β-lactamase (AmpC^D) 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: ジャーナルへの寄稿 › 学術論文 › 査読

10 被引用数 (Scopus)

抄録

The X-ray crystal structure of AmpC β-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 Å. 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 -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.

本文言語	英語
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
巻	65
号	6
DOI	https://doi.org/10.1107/S1744309109014249
出版ステータス	出版済み - 2009
外部発表	はい

All Science Journal Classification (ASJC) codes

生物理学
構造生物学
生化学
遺伝学
凝縮系物理学

文献へのアクセス

10.1107/S1744309109014249

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フィンガープリント

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引用スタイル

Yamaguchi, Y., Sato, G., Yamagata, Y., Doi, Y., Wachino, J. I., Arakawa, Y., Matsuda, K., & Kurosaki, H. (2009). Structure of AmpC β-lactamase (AmpC^D) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(6), 540-543. https://doi.org/10.1107/S1744309109014249

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

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.",

keywords = "AmpC β-lactamase, β-lactam antibiotics",

author = "Yoshihiro Yamaguchi and Genta Sato and Yuriko Yamagata and Yohei Doi and Wachino, \{Jun Ichi\} and Yoshichika Arakawa and Koki Matsuda and Hiromasa Kurosaki",

year = "2009",

doi = "10.1107/S1744309109014249",

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pages = "540--543",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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Yamaguchi, Y, Sato, G, Yamagata, Y, Doi, Y , Wachino, JI , Arakawa, Y, Matsuda, K & Kurosaki, H 2009, 'Structure of AmpC β-lactamase (AmpC^D) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 65, no. 6, pp. 540-543. https://doi.org/10.1107/S1744309109014249

Structure of AmpC β-lactamase (AmpC^D) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix. / Yamaguchi, Yoshihiro; Sato, Genta; Yamagata, Yuriko その他.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 6, 2009, p. 540-543.

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

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AU - Yamaguchi, Yoshihiro

AU - Sato, Genta

AU - Yamagata, Yuriko

AU - Doi, Yohei

AU - Wachino, Jun Ichi

AU - Arakawa, Yoshichika

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AU - Kurosaki, Hiromasa

PY - 2009

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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.

KW - AmpC β-lactamase

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