2NSE

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE SUBSTRATE COMPLEX

2NSE の概要

• エントリーDOI: 10.2210/pdb2nse/pdb
• 分子名称: NITRIC OXIDE SYNTHASE, CACODYLATE ION, ARGININE, ... (8 entities in total)
• 機能のキーワード: nitric oxide synthase, arginine, heme protein, tetrahydrobiopterin, complex (oxidoreductase-peptide), complex (oxidoreductase-peptide) complex, complex (oxidoreductase/peptide)
• 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: 101917.58

構造登録者

Raman, C.S.,Li, H.,Martasek, P.,Kral, V.,Masters, B.S.S.,Poulos, T.L. (登録日: 1998-08-13, 公開日: 1999-05-25, 最終更新日: 2024-02-21)

主引用文献

Raman, C.S.,Li, H.,Martasek, P.,Kral, V.,Masters, B.S.,Poulos, T.L.
Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.
Cell(Cambridge,Mass.), 95:939-950, 1998

PubMed Abstract: Nitric oxide, a key signaling molecule, is produced by a family of enzymes collectively called nitric oxide synthases (NOS). Here, we report the crystal structure of the heme domain of endothelial NOS in tetrahydrobiopterin (H4B)-free and -bound forms at 1.95 A and 1.9 A resolution, respectively. In both structures a zinc ion is tetrahedrally coordinated to pairs of symmetry-related cysteine residues at the dimer interface. The phylogenetically conserved Cys-(X)4-Cys motif and its strategic location establish a structural role for the metal center in maintaining the integrity of the H4B-binding site. The unexpected recognition of the substrate, L-arginine, at the H4B site indicates that this site is poised to stabilize a positively charged pterin ring and suggests a model involving a cationic pterin radical in the catalytic cycle.

PubMed: 9875848
DOI: 10.1016/S0092-8674(00)81718-3

実験手法

X-RAY DIFFRACTION (2.34 Å)