1FOO

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG AND NO(H4B-FREE)

1FOO の概要

• エントリーDOI: 10.2210/pdb1foo/pdb
• 関連するPDBエントリー: 4NSE
• 分子名称: NITRIC-OXIDE SYNTHASE, CACODYLATE ION, ACETATE ION, ... (9 entities in total)
• 機能のキーワード: alpha-beta fold, nitric oxide synthase, oxidoreductase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cell membrane: P29473
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101889.47

構造登録者

Raman, C.S.,Li, H.,Martasek, P.,Masters, B.S.S.,Poulos, T.L. (登録日: 2000-08-28, 公開日: 2001-07-20, 最終更新日: 2024-02-07)

主引用文献

Li, H.,Raman, C.S.,Martasek, P.,Masters, B.S.,Poulos, T.L.
Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors.
Biochemistry, 40:5399-5406, 2001

PubMed Abstract: The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.

PubMed: 11331003
DOI: 10.1021/bi002658v

実験手法

X-RAY DIFFRACTION (2 Å)