4IVK

Crystal structure of a fammily VIII carboxylesterase in a complex with cephalothin.

4IVK の概要

• エントリーDOI: 10.2210/pdb4ivk/pdb
• 関連するPDBエントリー: 4IVI
• 分子名称: Carboxylesterases, CEPHALOTHIN GROUP, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: helical domain and a alpha/beta domain, deep sea sediment, hydrolase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48190.91

構造登録者

An, Y.J.,Kim, M.-K.,Jeong, C.-S.,Cha, S.-S. (登録日: 2013-01-23, 公開日: 2013-06-19, 最終更新日: 2024-11-27)

主引用文献

Cha, S.S.,An, Y.J.,Jeong, C.S.,Kim, M.K.,Jeon, J.H.,Lee, C.M.,Lee, H.S.,Kang, S.G.,Lee, J.H.
Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase.
Proteins, 81:2045-2051, 2013

PubMed Abstract: EstU1 is a unique family VIII carboxylesterase that displays hydrolytic activity toward the amide bond of clinically used β-lactam antibiotics as well as the ester bond of p-nitrophenyl esters. EstU1 assumes a β-lactamase-like modular architecture and contains the residues Ser100, Lys103, and Tyr218, which correspond to the three catalytic residues (Ser64, Lys67, and Tyr150, respectively) of class C β-lactamases. The structure of the EstU1/cephalothin complex demonstrates that the active site of EstU1 is not ideally tailored to perform an efficient deacylation reaction during the hydrolysis of β-lactam antibiotics. This result explains the weak β-lactamase activity of EstU1 compared with class C β-lactamases. Finally, structural and sequential comparison of EstU1 with other family VIII carboxylesterases elucidates an operative molecular strategy used by family VIII carboxylesterases to extend their substrate spectrum.

PubMed: 23737193
DOI: 10.1002/prot.24334

実験手法

X-RAY DIFFRACTION (1.8 Å)