2BS2

QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

「1QLA」から置き換えられました

2BS2 の概要

• エントリーDOI: 10.2210/pdb2bs2/pdb
• 関連するPDBエントリー: 1E7P 1QLB 2BS3 2BS4
• 分子名称: QUINOL-FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT A, PROTOPORPHYRIN IX CONTAINING FE, DODECYL-BETA-D-MALTOSIDE, ... (12 entities in total)
• 機能のキーワード: oxidoreductase, respiratory chain, citric acid cycle, iron-sulphur protein
• 由来する生物種: WOLINELLA SUCCINOGENES; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 268107.79

構造登録者

Lancaster, C.R.D. (登録日: 2005-05-14, 公開日: 2006-10-25, 最終更新日: 2024-10-23)

主引用文献

Madej, M.G.,Nasiri, H.R.,Hilgendorff, N.S.,Schwalbe, H.,Lancaster, C.R.D.
Evidence for Transmembrane Proton Transfer in a Dihaem-Containing Membrane Protein Complex.
Embo J., 25:4963-, 2006

PubMed Abstract: Membrane protein complexes can support both the generation and utilisation of a transmembrane electrochemical proton potential ('proton-motive force'), either by transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane or by transmembrane proton transfer. Here we provide the first evidence that both of these mechanisms are combined in the case of a specific respiratory membrane protein complex, the dihaem-containing quinol:fumarate reductase (QFR) of Wolinella succinogenes, so as to facilitate transmembrane electron transfer by transmembrane proton transfer. We also demonstrate the non-functionality of this novel transmembrane proton transfer pathway ('E-pathway') in a variant QFR where a key glutamate residue has been replaced. The 'E-pathway', discussed on the basis of the 1.78-Angstrom-resolution crystal structure of QFR, can be concluded to be essential also for the viability of pathogenic epsilon-proteobacteria such as Helicobacter pylori and is possibly relevant to proton transfer in other dihaem-containing membrane proteins, performing very different physiological functions.

PubMed: 17024183
DOI: 10.1038/SJ.EMBOJ.7601361

実験手法

X-RAY DIFFRACTION (1.78 Å)