2DYS

Bovine heart cytochrome C oxidase modified by DCCD

2DYS の概要

• エントリーDOI: 10.2210/pdb2dys/pdb
• 関連するPDBエントリー: 1OCC 1OCO 1OCR 1OCZ 1V54 1V55 2dyr 2OCC
• 分子名称: Cytochrome c oxidase subunit 1, Cytochrome c oxidase polypeptide VIIa-heart, Cytochrome c oxidase polypeptide VIIb, ... (29 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Mitochondrion inner membrane; Multi-pass membrane protein: P00396 P68530 P00415; Mitochondrion inner membrane: P07470 P13183 P00430 P10175 P00423 P00426 P00428 P07471 P04038; Mitochondrion intermembrane space: P00429
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 443204.68

構造登録者

Shinzawa-Itoh, K.,Aoyama, H.,Muramoto, K.,Kurauchi, T.,Mizushima, T.,Yamashita, E.,Tsukihara, T.,Yoshikawa, S. (登録日: 2006-09-16, 公開日: 2007-04-03, 最終更新日: 2023-10-25)

主引用文献

Shinzawa-Itoh, K.,Aoyama, H.,Muramoto, K.,Terada, H.,Kurauchi, T.,Tadehara, Y.,Yamasaki, A.,Sugimura, T.,Kurono, S.,Tsujimoto, K.,Mizushima, T.,Yamashita, E.,Tsukihara, T.,Yoshikawa, S.
Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase
Embo J., 26:1713-1725, 2007

PubMed Abstract: All 13 lipids, including two cardiolipins, one phosphatidylcholine, three phosphatidylethanolamines, four phosphatidylglycerols and three triglycerides, were identified in a crystalline bovine heart cytochrome c oxidase (CcO) preparation. The chain lengths and unsaturated bond positions of the fatty acid moieties determined by mass spectrometry suggest that each lipid head group identifies its specific binding site within CcOs. The X-ray structure demonstrates that the flexibility of the fatty acid tails facilitates their effective space-filling functions and that the four phospholipids stabilize the CcO dimer. Binding of dicyclohexylcarbodiimide to the O(2) transfer pathway of CcO causes two palmitate tails of phosphatidylglycerols to block the pathway, suggesting that the palmitates control the O(2) transfer process.The phosphatidylglycerol with vaccenate (cis-Delta(11)-octadecenoate) was found in CcOs of bovine and Paracoccus denitrificans, the ancestor of mitochondrion, indicating that the vaccenate is conserved in bovine CcO in spite of the abundance of oleate (cis-Delta(9)-octadecenoate). The X-ray structure indicates that the protein moiety selects cis-vaccenate near the O(2) transfer pathway against trans-vaccenate. These results suggest that vaccenate plays a critical role in the O(2) transfer mechanism.

PubMed: 17332748
DOI: 10.1038/sj.emboj.7601618

実験手法

X-RAY DIFFRACTION (2.2 Å)