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New page: left|200px<br /><applet load="2an2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2an2, resolution 2.6Å" /> '''P332G, A333S Double m...
 
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[[Image:2an2.gif|left|200px]]<br /><applet load="2an2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2an2, resolution 2.6&Aring;" />
'''P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase'''<br />


==Overview==
==P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase==
Cooperativity among ligand binding, subunit association, and protein, folding has implications for enzyme regulation as well as protein, aggregation events associated with disease. The binding of substrate, l-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthases, (NOSs) from a "loose dimer", with an exposed active center and higher, sensitivity to proteolysis, to a "tight dimer" competent for catalysis., The crystallographic structure of the Bacillus subtilis NOS loose dimer, shows an altered association state with severely destabilized subdomains., Ligand binding or heme reduction converts loose dimers to tight dimers in, solution and crystals. Mutations at key positions in the dimer interface, that distinguish prokaryotic from eukaryotic NOSs affect the propensity to, form loose dimers. The loose dimer structure indicates that non-native, interactions can mediate subunit association in NOS.
<StructureSection load='2an2' size='340' side='right'caption='[[2an2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2an2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AN2 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=2an2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2an2 OCA], [https://pdbe.org/2an2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2an2 RCSB], [https://www.ebi.ac.uk/pdbsum/2an2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2an2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NOSO_BACSU NOSO_BACSU] Catalyzes the production of nitric oxide.
== 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/an/2an2_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=2an2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cooperativity among ligand binding, subunit association, and protein folding has implications for enzyme regulation as well as protein aggregation events associated with disease. The binding of substrate l-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthases (NOSs) from a "loose dimer", with an exposed active center and higher sensitivity to proteolysis, to a "tight dimer" competent for catalysis. The crystallographic structure of the Bacillus subtilis NOS loose dimer shows an altered association state with severely destabilized subdomains. Ligand binding or heme reduction converts loose dimers to tight dimers in solution and crystals. Mutations at key positions in the dimer interface that distinguish prokaryotic from eukaryotic NOSs affect the propensity to form loose dimers. The loose dimer structure indicates that non-native interactions can mediate subunit association in NOS.


==About this Structure==
Structure of a loose dimer: an intermediate in nitric oxide synthase assembly.,Pant K, Crane BR J Mol Biol. 2005 Sep 30;352(4):932-40. PMID:16126221<ref>PMID:16126221</ref>
2AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ARG, HEM and H4B 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=2AN2 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of a loose dimer: an intermediate in nitric oxide synthase assembly., Pant K, Crane BR, J Mol Biol. 2005 Sep 30;352(4):932-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16126221 16126221]
</div>
<div class="pdbe-citations 2an2" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Nitric-oxide synthase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Crane BR]]
[[Category: Crane, B.R.]]
[[Category: Pant K]]
[[Category: Pant, K.]]
[[Category: ARG]]
[[Category: H4B]]
[[Category: HEM]]
[[Category: double mutant]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:14:05 2007''

Latest revision as of 07:46, 13 August 2026

P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase

2an2, resolution 2.60Å

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