1fol: Difference between revisions

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-[[Image:1fol.gif|left|200px]]
- {{Structure
+==REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)==
-|PDB= 1fol |SIZE=350|CAPTION= <scene name='initialview01'>1fol</scene>, resolution 2.20&Aring;
+<StructureSection load='1fol' size='340' side='right'caption='[[1fol]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+<table><tr><td colspan='2'>[[1fol]] 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=1FOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOL FirstGlance]. <br>
-|ACTIVITY= [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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-|GENE=
+<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=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fol OCA], [https://pdbe.org/1fol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fol RCSB], [https://www.ebi.ac.uk/pdbsum/1fol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fol ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fol_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1fol ConSurf].
+<div style="clear:both"></div>
-'''REDUCED BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG(H4B-FREE)'''
+==See Also==
+*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.
-==About this Structure==
-FOL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOL OCA].
-==Reference==
-Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors., Li H, Raman CS, Martasek P, Masters BS, Poulos TL, Biochemistry. 2001 May 8;40(18):5399-406. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11331003 11331003]
 [[Category: Bos taurus]]
-[[Category: Nitric-oxide synthase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Li H]]
-[[Category: Li, H.]]
+[[Category: Martasek P]]
-[[Category: Martasek, P.]]
+[[Category: Masters BS]]
-[[Category: Masters, B S.]]
+[[Category: Poulos TL]]
-[[Category: Poulos, T L.]]
+[[Category: Raman CS]]
-[[Category: Raman, C S.]]
-[[Category: ACT]]
-[[Category: ARG]]
-[[Category: CAC]]
-[[Category: GOL]]
-[[Category: HEM]]
-[[Category: ZN]]
-[[Category: alpha-beta fold]]
-[[Category: nitric oxide synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:53 2008''