4KEP

Crystal structure of 4-pyridoxolactonase, wild-type

「3AJ0」から置き換えられました

4KEP の概要

• エントリーDOI: 10.2210/pdb4kep/pdb
• 関連するPDBエントリー: 3AJ3 4KEQ
• 分子名称: 4-pyridoxolactonase, ZINC ION, ACETATE ION, ... (7 entities in total)
• 機能のキーワード: alpha-beta/beta-alpha fold, hydrolase, lactone
• 由来する生物種: Mesorhizobium loti
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31291.32

構造登録者

Kobayashi, J.,Yoshikane, Y.,Baba, S.,Mizutani, K.,Takahashi, N.,Mikami, B.,Yagi, T. (登録日: 2013-04-26, 公開日: 2014-04-09, 最終更新日: 2023-11-08)

主引用文献

Kobayashi, J.,Yoshikane, Y.,Yagi, T.,Baba, S.,Mizutani, K.,Takahashi, N.,Mikami, B.
Structure of 4-pyridoxolactonase from Mesorhizobium loti.
Acta Crystallogr.,Sect.F, 70:424-432, 2014

PubMed Abstract: 4-Pyridoxolactonase from Mesorhizobium loti catalyzes the zinc-dependent lactone-ring hydrolysis of 4-pyridoxolactone (4PAL) to 4-pyridoxic acid (4PA) in vitamin B6 degradation pathway I. The crystal structures of 4-pyridoxolactonase and its complex with 5-pyridoxolactone (5PAL; the competitive inhibitor) were determined. The overall structure was an αβ/βα sandwich fold, and two zinc ions were coordinated. This strongly suggested that the enzyme belongs to subclass B3 of the class B β-lactamases. In the complex structure, the carbonyl group of 5PAL pointed away from the active site, revealing why it acts as a competitive inhibitor. Based on docking simulation with 4PAL, 4PA and a reaction intermediate, 4-pyridoxolactonase probably catalyzes the reaction through a subclass B2-like mechanism, not the subclass B3 mechanism.

PubMed: 24699732
DOI: 10.1107/S2053230X14003926

実験手法

X-RAY DIFFRACTION (1.83 Å)