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New page: left|200px<br /><applet load="1mjt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mjt, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1mjt.gif|left|200px]]<br /><applet load="1mjt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mjt, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU'''<br />


==Overview==
==CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU==
Prokaryotic genes related to the oxygenase domain of mammalian nitric, oxide synthases (NOSs) have recently been identified. Although they, catalyze the same reaction as the eukaryotic NOS oxygenase domain, their, biological function(s) are unknown. In order to explore rationally the, biochemistry and evolution of the prokaryotic NOS family, we have, determined the crystal structure of SANOS, from methicillin-resistant, Staphylococcus aureus (MRSA), to 2.4 A. Haem and S-ethylisothiourea, (SEITU) are bound at the SANOS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H(4)B) in mammalian, NOSs, has NAD(+) bound in SANOS. In common with all bacterial NOSs, SANOS, lacks the N-terminal extension responsible for stable dimerization in, mammalian isoforms, but has alternative interactions to promote dimer, formation.
<StructureSection load='1mjt' size='340' side='right'caption='[[1mjt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mjt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJT 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ITU:ETHYLISOTHIOUREA'>ITU</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</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=1mjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjt OCA], [https://pdbe.org/1mjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mjt RCSB], [https://www.ebi.ac.uk/pdbsum/1mjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mjt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NOSO_STAAU NOSO_STAAU] Catalyzes the production of nitric oxide (By similarity).
== 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/mj/1mjt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1mjt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prokaryotic genes related to the oxygenase domain of mammalian nitric oxide synthases (NOSs) have recently been identified. Although they catalyze the same reaction as the eukaryotic NOS oxygenase domain, their biological function(s) are unknown. In order to explore rationally the biochemistry and evolution of the prokaryotic NOS family, we have determined the crystal structure of SANOS, from methicillin-resistant Staphylococcus aureus (MRSA), to 2.4 A. Haem and S-ethylisothiourea (SEITU) are bound at the SANOS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H(4)B) in mammalian NOSs, has NAD(+) bound in SANOS. In common with all bacterial NOSs, SANOS lacks the N-terminal extension responsible for stable dimerization in mammalian isoforms, but has alternative interactions to promote dimer formation.


==About this Structure==
Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus.,Bird LE, Ren J, Zhang J, Foxwell N, Hawkins AR, Charles IG, Stammers DK Structure. 2002 Dec;10(12):1687-96. PMID:12467576<ref>PMID:12467576</ref>
1MJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with SUC, HEM, ITU and NAD 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=1MJT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus., Bird LE, Ren J, Zhang J, Foxwell N, Hawkins AR, Charles IG, Stammers DK, Structure. 2002 Dec;10(12):1687-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12467576 12467576]
</div>
[[Category: Nitric-oxide synthase]]
<div class="pdbe-citations 1mjt" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Bird, L.E.]]
[[Category: Bird LE]]
[[Category: Ren, J.]]
[[Category: Ren J]]
[[Category: Stammers, D.K.]]
[[Category: Stammers DK]]
[[Category: HEM]]
[[Category: ITU]]
[[Category: NAD]]
[[Category: SUC]]
[[Category: bacterial]]
[[Category: mrsa]]
[[Category: no]]
[[Category: nos]]
[[Category: sanos]]
[[Category: seitu]]
[[Category: staphylococcus aureus]]
[[Category: synthase]]
 
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