5EXD

Crystal structure of oxalate oxidoreductase from Moorella thermoacetica bound with carboxy-di-oxido-methyl-TPP (COOM-TPP) intermediate

5EXD の概要

• エントリーDOI: 10.2210/pdb5exd/pdb
• 関連するPDBエントリー: 5EXE
• 分子名称: Oxalate oxidoreductase subunit alpha, Oxalate oxidoreductase subunit delta, Oxalate oxidoreductase subunit beta, ... (8 entities in total)
• 機能のキーワード: oxalate, oxidoreductase, ofor, thiamine
• 由来する生物種: Moorella thermoacetica (strain ATCC 39073); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 454010.90

構造登録者

Gibson, M.I.,Chen, P.Y.-T.,Drennan, C.L. (登録日: 2015-11-23, 公開日: 2015-12-30, 最終更新日: 2023-09-27)

主引用文献

Gibson, M.I.,Chen, P.Y.,Johnson, A.C.,Pierce, E.,Can, M.,Ragsdale, S.W.,Drennan, C.L.
One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography.
Proc.Natl.Acad.Sci.USA, 113:320-325, 2016

PubMed Abstract: Thiamine pyrophosphate (TPP)-dependent oxalate oxidoreductase (OOR) metabolizes oxalate, generating two molecules of CO2 and two low-potential electrons, thus providing both the carbon and reducing equivalents for operation of the Wood-Ljungdahl pathway of acetogenesis. Here we present structures of OOR in which two different reaction intermediate bound states have been trapped: the covalent adducts between TPP and oxalate and between TPP and CO2. These structures, along with the previously determined structure of substrate-free OOR, allow us to visualize how active site rearrangements can drive catalysis. Our results suggest that OOR operates via a bait-and-switch mechanism, attracting substrate into the active site through the presence of positively charged and polar residues, and then altering the electrostatic environment through loop and side chain movements to drive catalysis. This simple but elegant mechanism explains how oxalate, a molecule that humans and most animals cannot break down, can be used for growth by acetogenic bacteria.

PubMed: 26712008
DOI: 10.1073/pnas.1518537113

実験手法

X-RAY DIFFRACTION (2.5 Å)