2nod: Difference between revisions
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New page: left|200px<br /><applet load="2nod" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nod, resolution 2.6Å" /> '''MURINE INDUCIBLE NITR... |
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[[Image:2nod.jpg|left|200px]]<br /><applet load="2nod" size=" | [[Image:2nod.jpg|left|200px]]<br /><applet load="2nod" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2nod, resolution 2.6Å" /> | caption="2nod, resolution 2.6Å" /> | ||
'''MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND WATER BOUND IN ACTIVE CENTER'''<br /> | '''MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND WATER BOUND IN ACTIVE CENTER'''<br /> | ||
==Overview== | ==Overview== | ||
Crystal structures of the murine cytokine-inducible nitric oxide synthase | 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== | ==About this Structure== | ||
2NOD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4, HEM and H4B as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http:// | 2NOD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=H4B:'>H4B</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Nitric-oxide synthase]] | [[Category: Nitric-oxide synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arvai, A | [[Category: Arvai, A S.]] | ||
[[Category: Crane, B | [[Category: Crane, B R.]] | ||
[[Category: Getzoff, E | [[Category: Getzoff, E D.]] | ||
[[Category: Stuehr, D | [[Category: Stuehr, D J.]] | ||
[[Category: Tainer, J | [[Category: Tainer, J A.]] | ||
[[Category: H4B]] | [[Category: H4B]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:06 2008'' | ||
