1nse
From Proteopedia
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BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
Overview
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.
About this Structure
1NSE is a Single protein structure of sequence from Bos taurus with , , , , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
Reference
Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center., Raman CS, Li H, Martasek P, Kral V, Masters BS, Poulos TL, Cell. 1998 Dec 23;95(7):939-50. PMID:9875848
Page seeded by OCA on Thu Feb 21 14:09:27 2008
Categories: Bos taurus | Nitric-oxide synthase | Single protein | Kral, V. | Li, H. | Martasek, P. | Masters, B S.S. | Poulos, T L. | Raman, C S. | ACT | CAC | GOL | H4B | HEM | ITU | ZN | Arginine | Heme protein | Nitric oxide synthase | Oxidoreductase | Tetrahydrobiopterin
