1FFT

The structure of ubiquinol oxidase from Escherichia coli

1FFT の概要

• エントリーDOI: 10.2210/pdb1fft/pdb
• 分子名称: UBIQUINOL OXIDASE, COPPER (II) ION, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total)
• 機能のキーワード: electron transport, cytochrome oxidase, membrane protein, oxidoreductase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 285655.15

構造登録者

Abramson, J.,Riistama, S.,Larsson, G.,Jasaitis, A.,Svensson-Ek, M.,Puustinen, A.,Iwata, S.,Wikstrom, M. (登録日: 2000-07-26, 公開日: 2000-10-18, 最終更新日: 2024-02-07)

主引用文献

Abramson, J.,Riistama, S.,Larsson, G.,Jasaitis, A.,Svensson-Ek, M.,Laakkonen, L.,Puustinen, A.,Iwata, S.,Wikstrom, M.
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site.
Nat.Struct.Biol., 7:910-917, 2000

PubMed Abstract: Cell respiration is catalyzed by the heme-copper oxidase superfamily of enzymes, which comprises cytochrome c and ubiquinol oxidases. These membrane proteins utilize different electron donors through dissimilar access mechanisms. We report here the first structure of a ubiquinol oxidase, cytochrome bo3, from Escherichia coli. The overall structure of the enzyme is similar to those of cytochrome c oxidases; however, the membrane-spanning region of subunit I contains a cluster of polar residues exposed to the interior of the lipid bilayer that is not present in the cytochrome c oxidase. Mutagenesis studies on these residues strongly suggest that this region forms a quinone binding site. A sequence comparison of this region with known quinone binding sites in other membrane proteins shows remarkable similarities. In light of these findings we suggest specific roles for these polar residues in electron and proton transfer in ubiquinol oxidase.

PubMed: 11017202
DOI: 10.1038/82824

実験手法

X-RAY DIFFRACTION (3.5 Å)