2ZJ9

X-ray crystal structure of AmpC beta-Lactamase (AmpC(D)) from an Escherichia coli with a Tripeptide Deletion (Gly286 Ser287 Asp288) on the H10 Helix

2ZJ9 の概要

• エントリーDOI: 10.2210/pdb2zj9/pdb
• 分子名称: AmpC, SODIUM ION, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: lactamase, tripeptide deletion, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79022.11

構造登録者

Yamaguchi, Y.,Sato, G.,Yamagata, Y.,Wachino, J.,Arakawa, Y.,Kurosaki, H. (登録日: 2008-02-29, 公開日: 2009-03-10, 最終更新日: 2023-11-01)

主引用文献

Yamaguchi, Y.,Sato, G.,Yamagata, Y.,Doi, Y.,Wachino, J.,Arakawa, Y.,Matsuda, K.,Kurosaki, H.
Structure of AmpC beta-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix
Acta Crystallogr.,Sect.F, 65:540-543, 2009

PubMed Abstract: The X-ray crystal structure of AmpC beta-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 A. 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 alpha-helix present in the native AmpC beta-lactamase of E. coli to a loop structure, which results in a widening of the substrate-binding site.

PubMed: 19478427
DOI: 10.1107/S1744309109014249

実験手法

X-RAY DIFFRACTION (1.7 Å)