5UJ4

Crystal structure of the KPC-2 beta-lactamase complexed with hydrolyzed faropenem

5UJ4 の概要

• エントリーDOI: 10.2210/pdb5uj4/pdb
• 関連するPDBエントリー: 5UJ3 5UL8
• 分子名称: Carbapenem-hydrolyzing beta-lactamase KPC, (2R)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-5-[(2R)-oxolan-2-yl]-2,3-dihydro-1,3-thiazole-4-carboxylic acid, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: carbapenemase, faropenem, beta-lactamase, complex, hydrolase-antibiotic complex, hydrolase/antibiotic
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31202.06

構造登録者

Pemberton, O.A.,Chen, Y. (登録日: 2017-01-16, 公開日: 2017-04-26, 最終更新日: 2024-10-09)

主引用文献

Pemberton, O.A.,Zhang, X.,Chen, Y.
Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).
J. Med. Chem., 60:3525-3530, 2017

PubMed Abstract: Carbapenem-resistant Enterobacteriaceae are resistant to most β-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A β-lactamase. Here, we present the first product complex crystal structures of KPC-2 with β-lactam antibiotics containing hydrolyzed cefotaxime and faropenem. They provide experimental insights into substrate recognition by KPC-2 and its unique cephalosporinase/carbapenemase activity. These structures also represent the first product complexes for a wild-type serine β-lactamase, elucidating the product release mechanism of these enzymes in general.

PubMed: 28388065
DOI: 10.1021/acs.jmedchem.7b00158

実験手法

X-RAY DIFFRACTION (1.4 Å)