2nod

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spinqualitylabelsall models 2nod, resolution 2.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND WATER BOUND IN ACTIVE CENTER

Overview

Crystal structures of the murine cytokine-inducible nitric oxide synthase, oxygenase dimer with active-center water molecules, the substrate, L-arginine (L-Arg), or product analog thiocitrulline reveal how, dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the, catalytic center for synthesis of the essential biological signal and, cytotoxin nitric oxide. Pterin binding refolds the central interface, region, recruits new structural elements, creates a 30 angstrom deep, active-center channel, and causes a 35 degrees helical tilt to expose a, heme edge and the adjacent residue tryptophan-366 for likely reductase, domain interactions and caveolin inhibition. Heme propionate interactions, with pterin and L-Arg suggest that pterin has electronic influences on, heme-bound oxygen. L-Arginine binds to glutamic acid-371 and stacks with, heme in an otherwise hydrophobic pocket to aid activation of heme-bound, oxygen by direct proton donation and thereby differentiate the two, chemical steps of nitric oxide synthesis.

About this Structure

2NOD is a Single protein structure of sequence from Mus musculus with SO4, HEM and H4B as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.

Reference

Structure of nitric oxide synthase oxygenase dimer with pterin and substrate., Crane BR, Arvai AS, Ghosh DK, Wu C, Getzoff ED, Stuehr DJ, Tainer JA, Science. 1998 Mar 27;279(5359):2121-6. PMID:9516116

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