2B10

Crystal Structure of the Protein-Protein Complex between F82S cytochrome c and cytochrome c peroxidase

2B10 の概要

• エントリーDOI: 10.2210/pdb2b10/pdb
• 関連するPDBエントリー: 2B0Z 2B11 2B12
• 分子名称: Cytochrome c peroxidase, mitochondrial, Cytochrome c iso-1, PROTOPORPHYRIN IX CONTAINING ZN, ... (5 entities in total)
• 機能のキーワード: cytochrome, electron transfer, 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
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93655.03

構造登録者

Kang, S.A.,Crane, B.R. (登録日: 2005-09-15, 公開日: 2005-10-25, 最終更新日: 2024-02-14)

主引用文献

Kang, S.A.,Crane, B.R.
Effects of interface mutations on association modes and electron-transfer rates between proteins
Proc.Natl.Acad.Sci.Usa, 102:15465-15470, 2005

PubMed Abstract: Although bonding networks determine electron-transfer (ET) rates within proteins, the mechanism by which structure and dynamics influence ET across protein interfaces is not well understood. Measurements of photochemically induced ET and subsequent charge recombination between Zn-porphyrin-substituted cytochrome c peroxidase and cytochrome c in single crystals correlate reactivity with defined structures for different association modes of the redox partners. Structures and ET rates in crystals are consistent with tryptophan oxidation mediating charge recombination reactions. Conservative mutations at the interface can drastically affect how the proteins orient and dispose redox centers. Whereas some configurations are ET inactive, the wild-type complex exhibits the fastest recombination rate. Other association modes generate ET rates that do not correlate with predictions based on cofactor separations or simple bonding pathways. Inhibition of photoinduced ET at <273 K indicates gating by small-amplitude dynamics, even within the crystal. Thus, different associations achieve states of similar reactivity, and within those states conformational fluctuations enable interprotein ET.

PubMed: 16227441
DOI: 10.1073/pnas.0505176102

実験手法

X-RAY DIFFRACTION (2.8 Å)