5EVY

Salicylate hydroxylase substrate complex

5EVY の概要

• エントリーDOI: 10.2210/pdb5evy/pdb
• 分子名称: Salicylate hydroxylase, FLAVIN-ADENINE DINUCLEOTIDE, 2-HYDROXYBENZOIC ACID, ... (4 entities in total)
• 機能のキーワード: complex, monooxygenase, oxidoreductase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48115.79

構造登録者

Morimoto, Y.,Uemura, T. (登録日: 2015-11-20, 公開日: 2015-12-16, 最終更新日: 2024-03-20)

主引用文献

Uemura, T.,Kita, A.,Watanabe, Y.,Adachi, M.,Kuroki, R.,Morimoto, Y.
The catalytic mechanism of decarboxylative hydroxylation of salicylate hydroxylase revealed by crystal structure analysis at 2.5 angstrom resolution
Biochem.Biophys.Res.Commun., 469:158-163, 2016

PubMed Abstract: The X-ray crystal structure of a salicylate hydroxylase from Pseudomonas putida S-1 complexed with coenzyme FAD has been determined to a resolution of 2.5 Å. Structural conservation with p- or m-hydroxybenzoate hydroxylase is very good throughout the topology, despite a low amino sequence identity of 20-40% between these three hydroxylases. Salicylate hydroxylase is composed of three distinct domains and includes FAD between domains I and II, which is accessible to solvent. In this study, which analyzes the tertiary structure of the enzyme, the unique reaction of salicylate, i.e. decarboxylative hydroxylation, and the structural roles of amino acids surrounding the substrate, are considered.

PubMed: 26616054
DOI: 10.1016/j.bbrc.2015.11.087

実験手法

X-RAY DIFFRACTION (2.47 Å)