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1d0c

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(New page: 200px<br /><applet load="1d0c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0c, resolution 1.65&Aring;" /> '''BOVINE ENDOTHELIAL N...)
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[[Image:1d0c.jpg|left|200px]]<br /><applet load="1d0c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d0c, resolution 1.65&Aring;" />
 
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'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-BROMO-7-NITROINDAZOLE (H4B FREE)'''<br />
 
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==Overview==
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==BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-BROMO-7-NITROINDAZOLE (H4B FREE)==
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Nitric oxide is generated under normal and pathophysiological conditions, by three distinct isoforms of nitric oxide synthase (NOS). A, small-molecule inhibitor of NOS (3-Br-7-nitroindazole, 7-NIBr) is, profoundly neuroprotective in mouse models of stroke and Parkinson's, disease. We report the crystal structure of the catalytic heme domain of, endothelial NOS complexed with 7-NIBr at 1.65 A resolution. Critical to, the binding of 7-NIBr at the substrate site is the adoption by eNOS of an, altered conformation, in which a key glutamate residue swings out toward, one of the heme propionate groups. Perturbation of the heme propionate, ensues and eliminates the cofactor tetrahydrobiopterin-heme interaction., We also present three crystal structures that reveal how alterations at, the substrate site facilitate 7-NIBr and structurally dissimilar ligands, to occupy the cofactor site.
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<StructureSection load='1d0c' size='340' side='right'caption='[[1d0c]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d0c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D0C FirstGlance]. <br>
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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]] 1.65&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAD:CACODYLIC+ACID'>CAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=INE:3-BROMO-7-NITROINDAZOLE'>INE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=1d0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0c OCA], [https://pdbe.org/1d0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d0c RCSB], [https://www.ebi.ac.uk/pdbsum/1d0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d0c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NOS3_BOVIN NOS3_BOVIN] Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.
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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/d0/1d0c_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=1d0c ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1D0C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ACT, ZN, HEM, INE, CAD and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D0C OCA].
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*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism., Raman CS, Li H, Martasek P, Southan G, Masters BS, Poulos TL, Biochemistry. 2001 Nov 13;40(45):13448-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11695891 11695891]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Nitric-oxide synthase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Li H]]
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[[Category: Li, H.]]
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[[Category: Martasek P]]
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[[Category: Martasek, P.]]
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[[Category: Masters BSS]]
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[[Category: Masters, B.S.S.]]
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[[Category: Poulos TL]]
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[[Category: Poulos, T.L.]]
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[[Category: Raman CS]]
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[[Category: Raman, C.S.]]
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[[Category: Southan GJ]]
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[[Category: Southan, G.J.]]
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[[Category: ACT]]
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[[Category: CAD]]
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[[Category: GOL]]
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[[Category: HEM]]
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[[Category: INE]]
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[[Category: ZN]]
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[[Category: alpha-beta fold]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:54:17 2007''
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Current revision

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-BROMO-7-NITROINDAZOLE (H4B FREE)

PDB ID 1d0c

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