2FU9

Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (mp2 inhibitor complex)

2FU9 の概要

• エントリーDOI: 10.2210/pdb2fu9/pdb
• 関連するPDBエントリー: 2FM6 2FU6 2FU7 2FU8
• 分子名称: Metallo-beta-lactamase L1, ZINC ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, zn, metallo, beta, lactamase, inhibitor
• 由来する生物種: Stenotrophomonas maltophilia
• 細胞内の位置: Periplasm (Potential): P52700
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59408.04

構造登録者

Nauton, L.,Garau, G.,Kahn, R.,Dideberg, O. (登録日: 2006-01-26, 公開日: 2007-01-30, 最終更新日: 2024-10-30)

主引用文献

Nauton, L.,Kahn, R.,Garau, G.,Hernandez, J.F.,Dideberg, O.
Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
J.Mol.Biol., 375:257-269, 2008

PubMed Abstract: One mechanism by which bacteria can escape the action of beta-lactam antibiotics is the production of metallo-beta-lactamases. Inhibition of these enzymes should restore the action of these widely used antibiotics. The tetrameric enzyme L1 from Stenotrophomonas maltophilia was used as a model system to determine a series of high-resolution crystal structures of apo, mono and bi-metal substituted proteins as well as protein-inhibitor complexes. Unexpectedly, although the apo structure revealed only few significant structural differences from the holo structure, some inhibitors were shown to induce amino acid side-chain rotations in the tightly packed active site. Moreover, one inhibitor employs a new binding mode in order to interact with the di-zinc center. This structural information could prove essential in the process of elucidation of the mode of interaction between a putative lead compound and metallo-beta-lactamases, one of the main steps in structure-based drug design.

PubMed: 17999929
DOI: 10.1016/j.jmb.2007.10.036

実験手法

X-RAY DIFFRACTION (1.8 Å)