1LL5

X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem

1LL5 の概要

• エントリーDOI: 10.2210/pdb1ll5/pdb
• 関連するPDBエントリー: 1BT5 1FCO 1KE4
• 分子名称: beta-lactamase, (5R)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-3-[(2-{[(E)-iminomethyl]amino}ethyl)sulfanyl]-4,5-dihydro-1H-pyrrole-2-carbox ylic acid (3 entities in total)
• 機能のキーワード: beta-lactamase, carbapenem, imipenem, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P00811
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79778.57

構造登録者

Beadle, B.M.,Shoichet, B.K. (登録日: 2002-04-26, 公開日: 2002-11-27, 最終更新日: 2024-11-20)

主引用文献

Beadle, B.M.,Shoichet, B.K.
Structural Basis for Imipenem Inhibition of Class C beta-lactamases
ANTIMICROB.AGENTS CHEMOTHER., 46:3978-3980, 2002

PubMed Abstract: To determine how imipenem inhibits the class C beta-lactamase AmpC, the X-ray crystal structure of the acyl-enzyme complex was determined to a resolution of 1.80 A. In the complex, the lactam carbonyl oxygen of imipenem has flipped by approximately 180 degrees compared to its expected position; the electrophilic acyl center is thus displaced from the point of hydrolytic attack. This conformation resembles that of imipenem bound to the class A enzyme TEM-1 but is different from that of moxalactam bound to AmpC.

PubMed: 12435704
DOI: 10.1128/AAC.46.12.3978-3980.2002

実験手法

X-RAY DIFFRACTION (1.8 Å)