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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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/"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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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>
<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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k1c|1k1c]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo1 OCA], [http://pdbe.org/1mo1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mo1 RCSB], [http://www.ebi.ac.uk/pdbsum/1mo1 PDBsum], [http://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 ==
[[http://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]]

Revision as of 09:01, 21 July 2021

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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