4V4C

Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici

これはPDB形式変換不可エントリーです。

4V4C の概要

• エントリーDOI: 10.2210/pdb4v4c/pdb
• 関連するPDBエントリー: 1TI4 1TI6 1VLE 1VLF
• 分子名称: Pyrogallol hydroxytransferase large subunit, Pyrogallol hydroxytransferase small subunit, ACETATE ION, ... (8 entities in total)
• 機能のキーワード: molybdenum binding enzyme, mgd-cofactors, dmso-reductase family, 4fe-4s-cluster, oxidoreductase
• 由来する生物種: Pelobacter acidigallici; 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1600925.95

構造登録者

Messerschmidt, A.,Niessen, H.,Abt, D.,Einsle, O.,Schink, B.,Kroneck, P.M.H. (登録日: 2004-06-02, 公開日: 2014-07-09, 最終更新日: 2024-02-28)

主引用文献

Messerschmidt, A.,Niessen, H.,Abt, D.,Einsle, O.,Schink, B.,Kroneck, P.M.H.
Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols
PROC.NATL.ACAD.SCI.USA, 101:11571-11576, 2004

PubMed Abstract: The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such trihydroxybenzenes and their derivatives represent important building blocks of plant polymers. None of the transferred hydroxyl groups originates from water during transhydroxylation; instead a cosubstrate, such as 1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron transfer. Here, we report on the crystal structure of the enzyme in the reduced Mo(IV) state, which we solved by single anomalous-diffraction technique. It represents the largest structure (1,149 amino acid residues per molecule, 12 independent molecules per unit cell), which has been solved so far by single anomalous-diffraction technique. Tranhydroxylase is a heterodimer, with the active Mo-molybdopterin guanine dinucleotide (MGD)(2) site in the alpha-subunit, and three [4Fe-4S] centers in the beta-subunit. The latter subunit carries a seven-stranded, mainly antiparallel beta-barrel domain. We propose a scheme for the transhydroxylation reaction based on 3D structures of complexes of the enzyme with various polyphenols serving either as substrate or inhibitor.

PubMed: 15284442
DOI: 10.1073/pnas.0404378101

実験手法

X-RAY DIFFRACTION (2.35 Å)