3DTU

Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides complexed with deoxycholic acid

3DTU の概要

• エントリーDOI: 10.2210/pdb3dtu/pdb
• 関連するPDBエントリー: 2GSM
• 分子名称: Cytochrome c oxidase subunit 1, TRIDECANE, CADMIUM ION, ... (14 entities in total)
• 機能のキーワード: transmembrane protein complex, deoxycholic acid, copper, electron transport, heme, hydrogen ion transport, ion transport, iron, membrane, metal-binding, oxidoreductase, respiratory chain, transmembrane, transport
• 由来する生物種: Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P33517 Q03736
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 198953.07

構造登録者

Qin, L.,Mills, D.A.,Buhrow, L.,Hiser, C.,Ferguson-Miller, S. (登録日: 2008-07-15, 公開日: 2008-09-16, 最終更新日: 2024-10-09)

主引用文献

Qin, L.,Mills, D.A.,Buhrow, L.,Hiser, C.,Ferguson-Miller, S.
A conserved steroid binding site in cytochrome C oxidase.
Biochemistry, 47:9931-9933, 2008

PubMed Abstract: Micromolar concentrations of the bile salt deoxycholate are shown to rescue the activity of an inactive mutant, E101A, in the K proton pathway of Rhodobacter sphaeroides cytochrome c oxidase. A crystal structure of the wild-type enzyme reveals, as predicted, deoxycholate bound with its carboxyl group at the entrance of the K path. Since cholate is a known potent inhibitor of bovine oxidase and is seen in a similar position in the bovine structure, the crystallographically defined, conserved steroid binding site could reveal a regulatory site for steroids or structurally related molecules that act on the essential K proton path.

PubMed: 18759498
DOI: 10.1021/bi8013483

実験手法

X-RAY DIFFRACTION (2.15 Å)