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[[Image:1ed6.gif|left|200px]]


{{Structure
==BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)==
|PDB= 1ed6 |SIZE=350|CAPTION= <scene name='initialview01'>1ed6</scene>, resolution 2.05&Aring;
<StructureSection load='1ed6' size='340' side='right'caption='[[1ed6]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <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=ILO:N5-IMINOETHYL-L-ORNITHINE'>ILO</scene>, <scene name='pdbligand=CAD:CACODYLIC+ACID'>CAD</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[1ed6]] 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=1ED6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ED6 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]] 2.05&#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=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=ILO:N5-IMINOETHYL-L-ORNITHINE'>ILO</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=1ed6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ed6 OCA], [https://pdbe.org/1ed6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ed6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ed6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ed6 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/ed/1ed6_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=1ed6 ConSurf].
<div style="clear:both"></div>


'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (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==
1ED6 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=1ED6 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: 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 BSS]]
[[Category: Masters, B S.S.]]
[[Category: Poulos TL]]
[[Category: Poulos, T L.]]
[[Category: Raman CS]]
[[Category: Raman, C S.]]
[[Category: Southan GJ]]
[[Category: Southan, G J.]]
[[Category: ACT]]
[[Category: CAD]]
[[Category: GOL]]
[[Category: HEM]]
[[Category: ILO]]
[[Category: ZN]]
[[Category: alpha-beta fold]]
[[Category: heme protein]]
[[Category: nitric oxide synthase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:53:57 2008''

Latest revision as of 10:01, 7 February 2024

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-NIO (H4B FREE)

Structural highlights

1ed6 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ed6, resolution 2.05Å

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OCA
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