1FOP

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

Summary for 1FOP

• Entry DOI: 10.2210/pdb1fop/pdb
• Related: 4NSE
• Descriptor: NITRIC-OXIDE SYNTHASE, CACODYLATE ION, ACETATE ION, ... (10 entities in total)
• Functional Keywords: alpha-beta fold, nitric oxide synthase, oxidoreductase
• Biological source: Bos taurus (cattle)
• Cellular location: Cell membrane: P29473
• Total number of polymer chains: 2
• Total formula weight: 102187.77

Authors

Raman, C.S.,Li, H.,Martasek, P.,Masters, B.S.S.,Poulos, T.L. (deposition date: 2000-08-28, release date: 2001-07-20, 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/bi002658v

Experimental method

X-RAY DIFFRACTION (2.3 Å)