1S6V

Structure of a cytochrome c peroxidase-cytochrome c site specific cross-link

1S6V の概要

• エントリーDOI: 10.2210/pdb1s6v/pdb
• 関連するPDBエントリー: 2PCC
• 分子名称: Cytochrome c peroxidase, mitochondrial, Cytochrome c, iso-1, IODIDE ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, heme enzyme, 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: 93834.96

構造登録者

Guo, M.,Bhaskar, B.,Li, H.,Barrows, T.P.,Poulos, T.L. (登録日: 2004-01-27, 公開日: 2004-04-27, 最終更新日: 2024-10-09)

主引用文献

Guo, M.,Bhaskar, B.,Li, H.,Barrows, T.P.,Poulos, T.L.
Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link
Proc.Natl.Acad.Sci.USA, 101:5940-5945, 2004

PubMed Abstract: A specific covalently cross-linked complex between redox partners yeast cytochrome c peroxidase (CCP) and cytochrome c (cyt. c) has been made by engineering cysteines into CCP and cyt. c that form an intermolecular disulfide bond in high yield. The crystal structure of the cross-linked complex has been solved to 1.88-A resolution and closely resembles the structure of the noncovalent complex [Pellitier, H. & Kraut, J. (1992) Science 258, 1748-1755]. The higher resolution of the covalent complex has enabled the location of ordered water molecules at the peroxidase-cytochrome c interface that serve to bridge between the two proteins by hydrogen bonding. As in the noncovalent complex, direct electrostatic interactions between protein groups appear not to be critical in complex formation. UV-visible spectroscopic and stopped-flow studies indicate that CCP in the covalent complex reacts normally with H(2)O(2) to give compound I. Stopped-flow kinetic studies also show that intramolecular electron transfer between the cross-linked ferrocytochrome c and the Trp-191 cation radical site in CCP compound I occurs fast and is nearly complete within the dead time ( approximately 2 ms) of the instrument. These results indicate that the structure of the covalent complex closely mimics the physiological electron transfer complex. In addition, single-turnover and steady-state experiments reveal that CCP compound I in the covalent complex oxidizes exogenously added ferrocytochrome c at a slow rate (t(1/2) approximately 2 min), indicating that CCP does not have a second independent site for physiologically relevant electron transfer.

PubMed: 15071191
DOI: 10.1073/pnas.0306708101

実験手法

X-RAY DIFFRACTION (1.88 Å)