1rzr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1rzr' size='340' side='right'caption='[[1rzr]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1rzr' size='340' side='right'caption='[[1rzr]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1rzr]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1rzr]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZR FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=1rzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzr OCA], [https://pdbe.org/1rzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rzr RCSB], [https://www.ebi.ac.uk/pdbsum/1rzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rzr ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/CCPA_PRIMG CCPA_PRIMG] Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1rzr ConSurf]. | </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=1rzr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Carbon catabolite repression (CCR) is one of the most fundamental environmental-sensing mechanisms in bacteria and imparts competitive advantage by establishing priorities in carbon metabolism. In gram-positive bacteria, the master transcription regulator of CCR is CcpA. CcpA is a LacI-GalR family member that employs, as an allosteric corepressor, the phosphoprotein HPr-Ser46-P, which is formed in glucose-replete conditions. Here we report structures of the Bacillus megaterium apoCcpA and a CcpA-(HPr-Ser46-P)-DNA complex. These structures reveal that HPr-Ser46-P mediates a novel two-component allosteric DNA binding activation mechanism that involves both rotation of the CcpA subdomains and relocation of pivot-point residue Thr61, which leads to juxtaposition of the DNA binding regions permitting "hinge" helix formation in the presence of cognate DNA. The structure of the CcpA-(HPr-Ser46-P)-cre complex also reveals the elegant mechanism by which CcpA family-specific interactions with HPr-Ser46-P residues Ser46-P and His15 partition the high-energy CCR and low-energy PTS pathways, the latter requiring HPr-His15-P. | ||
- | |||
- | Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P.,Schumacher MA, Allen GS, Diel M, Seidel G, Hillen W, Brennan RG Cell. 2004 Sep 17;118(6):731-41. PMID:15369672<ref>PMID:15369672</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1rzr" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Catabolite control protein 3D structures|Catabolite control protein 3D structures]] | *[[Catabolite control protein 3D structures|Catabolite control protein 3D structures]] | ||
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]] | *[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Atcc 14581]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Priestia megaterium]] |
- | [[Category: | + | [[Category: Allen GS]] |
- | [[Category: | + | [[Category: Brennan RG]] |
- | [[Category: | + | [[Category: Schumacher MA]] |
- | + | ||
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Revision as of 08:27, 1 May 2024
crystal structure of transcriptional regulator-phosphoprotein-DNA complex
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