1F26

CRYSTAL STRUCTURE OF NO COMPLEX OF THR243VAL MUTANTS OF CYTOCHROME P450NOR

1F26 の概要

• エントリーDOI: 10.2210/pdb1f26/pdb
• 関連するPDBエントリー: 1F24 1F25
• 分子名称: NITRIC OXIDE REDUCTASE, PROTOPORPHYRIN IX CONTAINING FE, NITRIC OXIDE, ... (5 entities in total)
• 機能のキーワード: nitric oxide reductase, cytochrome p450nor, oxidoreductase
• 由来する生物種: Fusarium oxysporum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45026.11

構造登録者

Shimizu, H.,Park, S.-Y. (登録日: 2000-05-23, 公開日: 2000-11-23, 最終更新日: 2024-05-29)

主引用文献

Obayashi, E.,Shimizu, H.,Park, S.Y.,Shoun, H.,Shiro, Y.
Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function.
J.Inorg.Biochem., 82:103-111, 2000

PubMed Abstract: Threonine 243 of cytochrome P450nor (fungal nitric oxide reductase) corresponds to the 'conserved' Thr in the long I helix of monooxygenase cytochrome P450s. In P450nor, the replacement of Thr243 with Asn, Ala or Val makes the enzymatic activity dramatically reduce. In order to understand the roles of Thr243 in the reduction reaction of NO by P450nor, the crystal structures of three Thr243 mutants (Thr243-->Asn, Thr243-->Val, Thr243-->Ala) of P450nor were determined at a 1.4-A resolution and at cryogenic temperature. However, the hydrogen-bonding pattern in the heme pocket of these mutants is essentially similar for that of the WT enzyme. This suggests that the determination of the structure of the NADH complex of P450nor is required, in order to evaluate the role of Thr243 in its enzymatic reaction. We attempted to crystallize the NADH complex under several conditions, but have not yet been successful.

PubMed: 11132616
DOI: 10.1016/S0162-0134(00)00161-6

実験手法

X-RAY DIFFRACTION (1.4 Å)