3NOD

MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND PRODUCT ANALOGUE L-THIOCITRULLINE

3NOD の概要

• エントリーDOI: 10.2210/pdb3nod/pdb
• 分子名称: NITRIC OXIDE SYNTHASE, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• 機能のキーワード: nitric oxide l-arginine monooxygenase, dimer, thiocitrulline nos, oxidoreductase
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 100191.41

構造登録者

Crane, B.R.,Arvai, A.S.,Getzoff, E.D.,Stuehr, D.J.,Tainer, J.A. (登録日: 1998-03-06, 公開日: 1999-03-23, 最終更新日: 2024-10-09)

主引用文献

Crane, B.R.,Arvai, A.S.,Ghosh, D.K.,Wu, C.,Getzoff, E.D.,Stuehr, D.J.,Tainer, J.A.
Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.
Science, 279:2121-2126, 1998

PubMed Abstract: 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.

PubMed: 9516116
DOI: 10.1126/science.279.5359.2121

実験手法

X-RAY DIFFRACTION (2.7 Å)