2X71

Structural basis for the interaction of lactivicins with serine beta- lactamases

2X71 の概要

• エントリーDOI: 10.2210/pdb2x71/pdb
• 分子名称: BETA-LACTAMASE, (2E)-2-{[(2S)-2-(ACETYLAMINO)-2-CARBOXYETHOXY]IMINO}PENTANEDIOIC ACID, ETHANOL, ... (5 entities in total)
• 機能のキーワード: hydrolase-antibiotic complex, antibiotic, hydrolase/antibiotic
• 由来する生物種: BACILLUS LICHENIFORMIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59597.17

構造登録者

Sauvage, E.,Herman, R.,Kerff, F.,Rocaboy, M.,Charlier, P. (登録日: 2010-02-22, 公開日: 2010-07-14, 最終更新日: 2024-11-13)

主引用文献

Brown, T.,Charlier, P.,Herman, R.,Schofield, C.J.,Sauvage, E.
Structural Basis for the Interaction of Lactivicins with Serine Beta-Lactamases.
J.Med.Chem., 53:5890-, 2010

PubMed Abstract: Lactivicin (LTV) is a natural non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases. A crystal structure of a BS3-LTV complex reveals that, as for its reaction with PBPs, LTV reacts with the nucleophilic serine and that cycloserine and lactone rings of LTV are opened. This structure, together with reported structures of PBP1b with lactivicins, provides a basis for developing improved lactivicin-based gamma-lactam antibiotics.

PubMed: 20593835
DOI: 10.1021/JM100437U

実験手法

X-RAY DIFFRACTION (2.1 Å)