1nos: Difference between revisions

New page: left|200px<br /><applet load="1nos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nos, resolution 2.1Å" /> '''MURINE INDUCIBLE NITR...
 
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'''MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), IMIDAZOLE COMPLEX'''<br />


==Overview==
==MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), IMIDAZOLE COMPLEX==
The nitric oxide synthase oxygenase domain (NOSox) oxidizes arginine to, synthesize the cellular signal and defensive cytotoxin nitric oxide (NO)., Crystal structures determined for cytokine-inducible NOSox reveal an, unusual fold and heme environment for stabilization of activated oxygen, intermediates key for catalysis. A winged beta sheet engenders a curved, alpha-beta domain resembling a baseball catcher's mitt with heme clasped, in the palm. The location of exposed hydrophobic residues and the results, of mutational analysis place the dimer interface adjacent to the, heme-binding pocket. Juxtaposed hydrophobic O2- and polar, L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors, and imply substrate-assisted catalysis.
<StructureSection load='1nos' size='340' side='right'caption='[[1nos]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nos]] is a 1 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=1NOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOS 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=1nos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nos OCA], [https://pdbe.org/1nos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nos RCSB], [https://www.ebi.ac.uk/pdbsum/1nos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nos ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/no/1nos_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=1nos ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with HEM and IMD 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=1NOS OCA].
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
 
== References ==
==Reference==
<references/>
The structure of nitric oxide synthase oxygenase domain and inhibitor complexes., Crane BR, Arvai AS, Gachhui R, Wu C, Ghosh DK, Getzoff ED, Stuehr DJ, Tainer JA, Science. 1997 Oct 17;278(5337):425-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9334294 9334294]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Nitric-oxide synthase]]
[[Category: Arvai AS]]
[[Category: Single protein]]
[[Category: Crane BR]]
[[Category: Arvai, A.S.]]
[[Category: Getzoff ED]]
[[Category: Crane, B.R.]]
[[Category: Stuehr DJ]]
[[Category: Getzoff, E.D.]]
[[Category: Tainer JA]]
[[Category: Stuehr, D.J.]]
[[Category: Tainer, J.A.]]
[[Category: HEM]]
[[Category: IMD]]
[[Category: heme]]
[[Category: imidazole]]
[[Category: l-arginine monooxygenase]]
[[Category: nitric oxide]]
[[Category: no]]
[[Category: nos]]
[[Category: oxidoreductase]]
 
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