4NFG

K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex

4NFG の概要

• エントリーDOI: 10.2210/pdb4nfg/pdb
• 分子名称: Cytochrome c peroxidase, mitochondrial, Cytochrome c, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• 機能のキーワード: oxidoreductase/electron transport, oxidoreductase-electron transport complex
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Mitochondrion matrix: P00431; Mitochondrion intermembrane space: P00004
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46541.85

構造登録者

Meulenbroek, E.M.,Bashir, Q.,Ubbink, M.,Pannu, N.S. (登録日: 2013-10-31, 公開日: 2014-09-24, 最終更新日: 2024-11-27)

主引用文献

Bashir, Q.,Meulenbroek, E.M.,Pannu, N.S.,Ubbink, M.
Engineering specificity in a dynamic protein complex with a single conserved mutation.
Febs J., 281:4892-4905, 2014

PubMed Abstract: It has been demonstrated that the complex of yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP) exists as a delicate equilibrium of a specific, active state and the non-specific, dynamic encounter state. An ortholog of yeast Cc, horse Cc, binds CcP but forms a much more dynamic complex, as demonstrated by NMR spectroscopy. A single conservative mutation of lysine 13 to arginine reduces the dynamics and enhances the specificity. The crystal structure of the stereospecific complex resembles the yeast Cc-CcP complex. In contrast, the K13A mutation increases the dynamic nature of the complex with CcP, showing that specificity in a redox protein complex can depend on the interactions of a single side chain in the binding interface.

PubMed: 25180929
DOI: 10.1111/febs.13028

実験手法

X-RAY DIFFRACTION (2.11 Å)