2YEV

Structure of caa3-type cytochrome oxidase

2YEV の概要

• エントリーDOI: 10.2210/pdb2yev/pdb
• 分子名称: CYTOCHROME C OXIDASE POLYPEPTIDE I+III, DINUCLEAR COPPER ION, HEME C, ... (14 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: THERMUS THERMOPHILUS; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 277440.95

構造登録者

Lyons, J.A.,Aragao, D.,Soulimane, T.,Caffrey, M. (登録日: 2011-03-31, 公開日: 2012-05-23, 最終更新日: 2024-11-13)

主引用文献

Lyons, J.A.,Aragao, D.,Slattery, O.,Pisliakov, A.V.,Soulimane, T.,Caffrey, M.
Structural Insights Into Electron Transfer in Caa3-Type Cytochrome Oxidases.
Nature, 487:514-, 2012

PubMed Abstract: Cytochrome c oxidase is a member of the haem copper oxidase superfamily (HCO). HCOs function as the terminal enzymes in the respiratory chain of mitochondria and aerobic prokaryotes, coupling molecular oxygen reduction to transmembrane proton pumping. Integral to the enzyme's function is the transfer of electrons from cytochrome c to the oxidase via a transient association of the two proteins. Electron entry and exit are proposed to occur from the same site on cytochrome c. Here we report the crystal structure of the caa3-type cytochrome oxidase from Thermus thermophilus, which has a covalently tethered cytochrome c domain. Crystals were grown in a bicontinuous mesophase using a synthetic short-chain monoacylglycerol as the hosting lipid. From the electron density map, at 2.36 Å resolution, a novel integral membrane subunit and a native glycoglycerophospholipid embedded in the complex were identified. Contrary to previous electron transfer mechanisms observed for soluble cytochrome c, the structure reveals the architecture of the electron transfer complex for the fused cupredoxin/cytochrome c domain, which implicates different sites on cytochrome c for electron entry and exit. Support for an alternative to the classical proton gate characteristic of this HCO class is presented.

PubMed: 22763450
DOI: 10.1038/NATURE11182

実験手法

X-RAY DIFFRACTION (2.36 Å)