2oen

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{{Seed}}
 
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[[Image:2oen.png|left|200px]]
 
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==Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose-6-phosphate and fructose-1,6-bisphosphate==
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The line below this paragraph, containing "STRUCTURE_2oen", creates the "Structure Box" on the page.
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<StructureSection load='2oen' size='340' side='right'caption='[[2oen]], [[Resolution|resolution]] 3.17&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2oen]] is a 2 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=2OEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OEN FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.17&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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{{STRUCTURE_2oen| PDB=2oen | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oen OCA], [https://pdbe.org/2oen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oen RCSB], [https://www.ebi.ac.uk/pdbsum/2oen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oen ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oe/2oen_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2oen ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In Gram-positive bacteria, carbon catabolite regulation (CCR) is mediated by the carbon catabolite control protein A (CcpA), a member of the LacI-GalR family of transcription regulators. Unlike other LacI-GalR proteins, CcpA is activated to bind DNA by binding the phosphoproteins HPr-Ser46-P or Crh-Ser46-P. However, fine regulation of CCR is accomplished by the small molecule effectors, glucose 6-phosphate (G6P) and fructose 1,6-bisphosphate (FBP), which somehow enhance CcpA-(HPr-Ser46-P) binding to DNA. Unlike the CcpA-(HPr-Ser46-P) complex, DNA binding by CcpA-(Crh-Ser46-P) is not stimulated by G6P or FBP. To understand the fine-tuning mechanism of these effectors, we solved the structures of the CcpA core, DeltaCcpA, which lacks the N-terminal DNA-binding domain, in complex with HPr-Ser46-P and G6P or FBP. G6P and FBP bind in a deep cleft, between the N and C subdomains of CcpA. Neither interacts with HPr-Ser46-P. This suggests that one role of the adjunct corepressors is to buttress the DNA-binding conformation effected by the binding of HPr-Ser46-P to the CcpA dimer N subdomains. However, the structures reveal that an unexpected function of adjunct corepressor binding is to bolster cross interactions between HPr-Ser46-P residue Arg17 and residues Asp69 and Asp99 of the other CcpA subunit. These cross contacts, which are weak or not present in the CcpA-(Crh-Ser46-P) complex, stimulate the CcpA-(HPr-Ser46-P)-DNA interaction specifically. Thus, stabilization of the closed conformation and bolstering of cross contacts between CcpA and its other corepressor, HPr-Ser46-P, provide a molecular explanation for how adjunct corepressors G6P and FBP enhance the interaction between CcpA-(HPr-Ser46-P) and cognate DNA.
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===Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose-6-phosphate and fructose-1,6-bisphosphate===
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Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate.,Schumacher MA, Seidel G, Hillen W, Brennan RG J Mol Biol. 2007 May 11;368(4):1042-50. Epub 2007 Feb 27. PMID:17376479<ref>PMID:17376479</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2oen" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17376479}}, adds the Publication Abstract to the page
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*[[Catabolite control protein 3D structures|Catabolite control protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17376479 is the PubMed ID number.
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*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_17376479}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2OEN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OEN OCA].
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[[Category: Large Structures]]
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[[Category: Priestia megaterium]]
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==Reference==
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[[Category: Brennan RG]]
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Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate., Schumacher MA, Seidel G, Hillen W, Brennan RG, J Mol Biol. 2007 May 11;368(4):1042-50. Epub 2007 Feb 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17376479 17376479]
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[[Category: Hillen W]]
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[[Category: Bacillus megaterium]]
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[[Category: Schumacher MA]]
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[[Category: Protein complex]]
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[[Category: Seidel G]]
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[[Category: Brennan, R G.]]
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[[Category: Hillen, W.]]
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[[Category: Schumacher, M A.]]
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[[Category: Seidel, G.]]
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[[Category: Adjunct corepressor]]
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[[Category: Ccpa]]
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[[Category: Ccr]]
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[[Category: Crh]]
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[[Category: Hpr]]
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[[Category: Protein-dna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:48:57 2008''
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Current revision

Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose-6-phosphate and fructose-1,6-bisphosphate

PDB ID 2oen

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