1NML

Di-haemic Cytochrome c Peroxidase from Pseudomonas nautica 617, form IN (pH 4.0)

1NML の概要

• エントリーDOI: 10.2210/pdb1nml/pdb
• 分子名称: di-haem cytochrome c peroxidase, HEME C, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, peroxidase, di-haem, electron transport
• 由来する生物種: Marinobacter hydrocarbonoclasticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37389.01

構造登録者

Dias, J.M.,Bonifacio, C.,Alves, T.,Pereira, A.S.,Bourgeois, D.,Moura, I.,Romao, M.J. (登録日: 2003-01-10, 公開日: 2004-01-13, 最終更新日: 2024-10-30)

主引用文献

Dias, J.M.,Alves, T.,Pereira, A.S.,Bourgeois, D.,Moura, I.
Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617
Structure, 12:961-973, 2004

PubMed Abstract: Cytochrome c peroxidase (CCP) catalyses the reduction of H(2)O(2) to H(2)O, an important step in the cellular detoxification process. The crystal structure of the di-heme CCP from Pseudomonas nautica 617 was obtained in two different conformations in a redox state with the electron transfer heme reduced. Form IN, obtained at pH 4.0, does not contain Ca(2+) and was refined at 2.2 A resolution. This inactive form presents a closed conformation where the peroxidatic heme adopts a six-ligand coordination, hindering the peroxidatic reaction from taking place. Form OUT is Ca(2+) dependent and was crystallized at pH 5.3 and refined at 2.4 A resolution. This active form shows an open conformation, with release of the distal histidine (His71) ligand, providing peroxide access to the active site. This is the first time that the active and inactive states are reported for a di-heme peroxidase.

PubMed: 15274917
DOI: 10.1016/j.str.2004.03.025

実験手法

X-RAY DIFFRACTION (2.2 Å)