1mo1: Difference between revisions

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[[Image:1mo1.jpg|left|200px]]<br /><applet load="1mo1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mo1, resolution 1.80&Aring;" />
'''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'''<br />


==About this Structure==
==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 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MO1 OCA].  
<StructureSection load='1mo1' size='340' side='right'caption='[[1mo1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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='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='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='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>
== 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>
== 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/mo/1mo1_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=1mo1 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Haser, R.]]
[[Category: Haser R]]
[[Category: Juy, M R.]]
[[Category: Juy MR]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: open-faced b-sandwich]]
[[Category: phosphotransferase system]]
[[Category: swapping domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:13 2008''