1mu4
From Proteopedia
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==CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)== | ==CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)== | ||
| - | <StructureSection load='1mu4' size='340' side='right' caption='[[1mu4]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1mu4' size='340' side='right'caption='[[1mu4]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1mu4]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1mu4]] is a 2 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=1MU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MU4 FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mu4 OCA], [https://pdbe.org/1mu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mu4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mu4 ProSAT]</span></td></tr> |
| - | <table> | + | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mu4_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mu4_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1mu4 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity. | ||
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| - | Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr.,Juy M, Penin F, Favier A, Galinier A, Montserret R, Haser R, Deutscher J, Bockmann A J Mol Biol. 2003 Sep 26;332(4):767-76. PMID:12972249<ref>PMID:12972249</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Haser R]] |
| - | [[Category: | + | [[Category: Juy MR]] |
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Current revision
CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)
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