1mo1: Difference between revisions

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<StructureSection load='1mo1' size='340' side='right'caption='[[1mo1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1mo1' size='340' side='right'caption='[[1mo1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mo1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MO1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mo1]] is a 4 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=1MO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MO1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k1c|1k1c]]</div></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=1mo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo1 OCA], [https://pdbe.org/1mo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mo1 ProSAT]</span></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=1mo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo1 OCA], [https://pdbe.org/1mo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mo1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CRH_BACSU CRH_BACSU]] Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.<ref>PMID:9237995</ref> <ref>PMID:16316990</ref>
[https://www.uniprot.org/uniprot/CRH_BACSU CRH_BACSU] Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.<ref>PMID:9237995</ref> <ref>PMID:16316990</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mo1_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mo1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Haser, R]]
[[Category: Haser R]]
[[Category: Juy, M R]]
[[Category: Juy MR]]
[[Category: Open-faced b-sandwich]]
[[Category: Phosphotransferase system]]
[[Category: Swapping domain]]
[[Category: Transport protein]]

Latest revision as of 07:01, 30 October 2024

CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF SELENO METHIONYLED CRH, THE BACILLUS SUBTILIS CATABOLITE REPRESSION CONTAINING PROTEIN CRH REVEALS AN UNEXPECTED SWAPPING DOMAIN AS AN UNTERTWINNED DIMER

1mo1, resolution 1.80Å

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