2N18

Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase

2N18 の概要

• エントリーDOI: 10.2210/pdb2n18/pdb
• 関連するPDBエントリー: 1S6V
• NMR情報: BMRB: 25551
• 分子名称: Cytochrome c peroxidase, mitochondrial, Cytochrome c iso-1, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: cytochrome c, cytochrome c peroxidase, low affinity complex, oxidoreductase-electron transport complex, oxidoreductase/electron transport
• 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: P00044 P00044
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 59544.35

構造登録者

Volkov, A.,Van de Water, K. (登録日: 2015-03-24, 公開日: 2015-05-13, 最終更新日: 2024-10-09)

主引用文献

Van de Water, K.,Sterckx, Y.G.,Volkov, A.N.
The low-affinity complex of cytochrome c and its peroxidase.
Nat Commun, 6:7073-7073, 2015

PubMed Abstract: The complex of yeast cytochrome c peroxidase and cytochrome c is a paradigm of the biological electron transfer (ET). Building on seven decades of research, two different models have been proposed to explain its functional redox activity. One postulates that the intermolecular ET occurs only in the dominant, high-affinity protein-protein orientation, while the other posits formation of an additional, low-affinity complex, which is much more active than the dominant one. Unlike the high-affinity interaction-extensively studied by X-ray crystallography and NMR spectroscopy-until now the binding of cytochrome c to the low-affinity site has not been observed directly, but inferred mainly from kinetics experiments. Here we report the structure of this elusive, weak protein complex and show that it consists of a dominant, inactive bound species and an ensemble of minor, ET-competent protein-protein orientations, which summarily account for the experimentally determined value of the ET rate constant.

PubMed: 25944250
DOI: 10.1038/ncomms8073

実験手法

SOLUTION NMR