2CC1

Crystal structure of the class A beta-lactamase from Mycobacterium fortuitum

「1MFO」から置き換えられました

2CC1 の概要

• エントリーDOI: 10.2210/pdb2cc1/pdb
• 分子名称: Beta-lactamase (2 entities in total)
• 機能のキーワード: hydrolase, antibiotic resistance, beta-lactamase, broad-spectrum, penicillin
• 由来する生物種: Mycolicibacterium fortuitum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28108.68

構造登録者

Sauvage, E.,Fonze, E.,Charlier, P. (登録日: 2006-01-11, 公開日: 2006-01-13, 最終更新日: 2023-12-13)

主引用文献

Sauvage, E.,Fonze, E.,Quinting, B.,Galleni, M.,Frere, J.M.,Charlier, P.
Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity.
Antimicrob. Agents Chemother., 50:2516-2521, 2006

PubMed Abstract: beta-Lactamases are the main cause of bacterial resistance to penicillins and cephalosporins. Class A beta-lactamases, the largest group of beta-lactamases, have been found in many bacterial strains, including mycobacteria, for which no beta-lactamase structure has been previously reported. The crystal structure of the class A beta-lactamase from Mycobacterium fortuitum (MFO) has been solved at 2.13-A resolution. The enzyme is a chromosomally encoded broad-spectrum beta-lactamase with low specific activity on cefotaxime. Specific features of the active site of the class A beta-lactamase from M. fortuitum are consistent with its specificity profile. Arg278 and Ser237 favor cephalosporinase activity and could explain its broad substrate activity. The MFO active site presents similarities with the CTX-M type extended-spectrum beta-lactamases but lacks a specific feature of these enzymes, the VNYN motif (residues 103 to 106), which confers on CTX-M-type extended-spectrum beta-lactamases a more efficient cefotaximase activity.

PubMed: 16801434
DOI: 10.1128/AAC.01226-05

実験手法

X-RAY DIFFRACTION (2.13 Å)