1d0o: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1d0o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0o, resolution 1.95Å" /> '''BOVINE ENDOTHELIAL N...
 
No edit summary
 
(18 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1d0o.jpg|left|200px]]<br /><applet load="1d0o" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1d0o, resolution 1.95&Aring;" />
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-BROMO-7-NITROINDAZOLE (H4B PRESENT)'''<br />


==Overview==
==BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-BROMO-7-NITROINDAZOLE (H4B PRESENT)==
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.
<StructureSection load='1d0o' size='340' side='right'caption='[[1d0o]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d0o]] 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=1D0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D0O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0o OCA], [https://pdbe.org/1d0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d0o RCSB], [https://www.ebi.ac.uk/pdbsum/1d0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d0o 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/d0/1d0o_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=1d0o ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1D0O 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=1D0O OCA].
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[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: INE]]
[[Category: ZN]]
[[Category: alpha-beta fold]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:54:58 2007''

Latest revision as of 09:47, 7 February 2024

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

Structural highlights

1d0o 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 1.95Å
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

1d0o, resolution 1.95Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1d0o&oldid=4041460"