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1df1

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[[Image:1df1.gif|left|200px]]
 
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==MURINE INOSOXY DIMER WITH ISOTHIOUREA BOUND IN THE ACTIVE SITE==
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The line below this paragraph, containing "STRUCTURE_1df1", creates the "Structure Box" on the page.
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<StructureSection load='1df1' size='340' side='right'caption='[[1df1]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1df1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DF1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ITU:ETHYLISOTHIOUREA'>ITU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1df1| PDB=1df1 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1df1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1df1 OCA], [https://pdbe.org/1df1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1df1 RCSB], [https://www.ebi.ac.uk/pdbsum/1df1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1df1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/1df1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1df1 ConSurf].
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<div style="clear:both"></div>
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'''MURINE INOSOXY DIMER WITH ISOTHIOUREA BOUND IN THE ACTIVE SITE'''
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==See Also==
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*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Nitric oxide synthase oxygenase domains (NOS(ox)) must bind tetrahydrobiopterin and dimerize to be active. New crystallographic structures of inducible NOS(ox) reveal that conformational changes in a switch region (residues 103-111) preceding a pterin-binding segment exchange N-terminal beta-hairpin hooks between subunits of the dimer. N-terminal hooks interact primarily with their own subunits in the 'unswapped' structure, and two switch region cysteines (104 and 109) from each subunit ligate a single zinc ion at the dimer interface. N-terminal hooks rearrange from intra- to intersubunit interactions in the 'swapped structure', and Cys109 forms a self-symmetric disulfide bond across the dimer interface. Subunit association and activity are adversely affected by mutations in the N-terminal hook that disrupt interactions across the dimer interface only in the swapped structure. Residue conservation and electrostatic potential at the NOS(ox) molecular surface suggest likely interfaces outside the switch region for electron transfer from the NOS reductase domain. The correlation between three-dimensional domain swapping of the N-terminal hook and metal ion release with disulfide formation may impact inducible nitric oxide synthase (i)NOS stability and regulation in vivo.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1DF1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF1 OCA].
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==Reference==
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N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization., Crane BR, Rosenfeld RJ, Arvai AS, Ghosh DK, Ghosh S, Tainer JA, Stuehr DJ, Getzoff ED, EMBO J. 1999 Nov 15;18(22):6271-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10562539 10562539]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Nitric-oxide synthase]]
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[[Category: Arvai AS]]
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[[Category: Single protein]]
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[[Category: Crane BR]]
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[[Category: Arvai, A S.]]
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[[Category: Getzoff ED]]
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[[Category: Crane, B R.]]
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[[Category: Ghosh DK]]
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[[Category: Getzoff, E D.]]
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[[Category: Ghosh S]]
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[[Category: Ghosh, D K.]]
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[[Category: Rosenfeld RJ]]
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[[Category: Ghosh, S.]]
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[[Category: Stuehr DJ]]
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[[Category: Rosenfeld, R J.]]
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[[Category: Tainer JA]]
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[[Category: Stuehr, D J.]]
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[[Category: Tainer, J A.]]
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[[Category: Heme]]
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[[Category: Ino]]
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[[Category: Isothiourea]]
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[[Category: Nitric oxide l-arginine monooxygenase]]
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[[Category: No]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:46:41 2008''
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Current revision

MURINE INOSOXY DIMER WITH ISOTHIOUREA BOUND IN THE ACTIVE SITE

PDB ID 1df1

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