5GMX

Crystal structure of a family VIII carboxylesterase

5GMX の概要

• エントリーDOI: 10.2210/pdb5gmx/pdb
• 分子名称: Carboxylesterase, phenylmethanesulfonic acid (3 entities in total)
• 機能のキーワード: estsrt1, extended spectrum beta-lactamase activity, flexibility, hydrolase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87156.72

構造登録者

An, Y.J.,Cha, S.S. (登録日: 2016-07-18, 公開日: 2017-07-26, 最終更新日: 2024-10-23)

主引用文献

Cha, S.S.,An, Y.J.
Crystal structure of EstSRT1, a family VIII carboxylesterase displaying hydrolytic activity toward oxyimino cephalosporins
Biochem. Biophys. Res. Commun., 478:818-824, 2016

PubMed Abstract: EstSRT1 is a family VIII carboxylesterase that hydrolyzes oxyimino third- and fourth-generation cephalosporins, first-generation cephalosporins and ester substrates. According to the crystal structure of EstSRT1 (2.0-Å resolution), this protein contains a large α/β domain and a small α-helical domain and harbors three catalytic residues (Ser71, Lys74, and Tyr160) in the cavity at the domain interface, similarly to other family VIII carboxylesterases. Comparison of the structures of EstSRT1 and EstU1, a family VIII carboxylesterase with no hydrolytic activity toward bulky oxyimino cephalosporins, revealed that EstSRT1 has a smaller active site, despite its extended substrate range. The B-factors of the active site segments that could potentially contact with the oxyimino groups and the R2 side chains of oxyimino cephalosporins are higher in EstSRT1 than in EstU1, thus suggesting the role of the active site's structural flexibility in the extension of EstSRT1's substrate spectrum.

PubMed: 27501751
DOI: 10.1016/j.bbrc.2016.08.031

実験手法

X-RAY DIFFRACTION (2 Å)