1ED6

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)

Summary for 1ED6

• Entry DOI: 10.2210/pdb1ed6/pdb
• Related: 1ED4 1ED5 1NSE
• Descriptor: NITRIC OXIDE SYNTHASE, ACETATE ION, ZINC ION, ... (8 entities in total)
• Functional Keywords: nitric oxide synthase, heme protein, alpha-beta fold, oxidoreductase
• Biological source: Bos taurus (cattle)
• Cellular location: Cell membrane: P29473
• Total number of polymer chains: 2
• Total formula weight: 101643.29

Authors

Raman, C.S.,Li, H.,Martasek, P.,Southan, G.J.,Masters, B.S.S.,Poulos, T.L. (deposition date: 2000-01-26, release date: 2001-01-31, Last modification date: 2024-02-07)

Primary citation

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/bi010957u

Experimental method

X-RAY DIFFRACTION (2.05 Å)