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2fep

From Proteopedia

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Current revision (09:25, 30 August 2023) (edit) (undo)
 
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<StructureSection load='2fep' size='340' side='right'caption='[[2fep]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='2fep' size='340' side='right'caption='[[2fep]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2fep]] is a 2 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=2FEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2fep]] 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=2FEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEP FirstGlance]. <br>
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</td></tr><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>
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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]] 2.45&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rzr|1rzr]], [[1sxg|1sxg]], [[1sxh|1sxh]], [[1shi|1shi]], [[2ak7|2ak7]], [[1zvv|1zvv]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ccpA, alsA, amyR, graR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835]), ptsH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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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=2fep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fep OCA], [https://pdbe.org/2fep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fep RCSB], [https://www.ebi.ac.uk/pdbsum/2fep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fep 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=2fep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fep OCA], [https://pdbe.org/2fep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fep RCSB], [https://www.ebi.ac.uk/pdbsum/2fep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fep ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CCPA_BACSU CCPA_BACSU]] Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons.<ref>PMID:1904524</ref> <ref>PMID:7665492</ref> <ref>PMID:10559165</ref> <ref>PMID:11557150</ref> <ref>PMID:21106498</ref> [[https://www.uniprot.org/uniprot/PTHP_BACSU PTHP_BACSU]] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).<ref>PMID:8195089</ref> <ref>PMID:8596444</ref> P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity.<ref>PMID:8195089</ref> <ref>PMID:8596444</ref>
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[https://www.uniprot.org/uniprot/CCPA_BACSU CCPA_BACSU] Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons.<ref>PMID:1904524</ref> <ref>PMID:7665492</ref> <ref>PMID:10559165</ref> <ref>PMID:11557150</ref> <ref>PMID:21106498</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Vibrio subtilis ehrenberg 1835]]
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[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chaptal, V]]
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[[Category: Chaptal V]]
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[[Category: Deutscher, J]]
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[[Category: Deutscher J]]
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[[Category: Galinier, A]]
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[[Category: Galinier A]]
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[[Category: Gueguen-Chaignon, V]]
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[[Category: Gueguen-Chaignon V]]
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[[Category: Lecampion, C]]
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[[Category: Lecampion C]]
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[[Category: Meyer, P]]
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[[Category: Meyer P]]
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[[Category: Nessler, S]]
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[[Category: Nessler S]]
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[[Category: Poncet, S]]
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[[Category: Poncet S]]
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[[Category: Ccpa]]
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[[Category: Hpr]]
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[[Category: Transcription]]
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[[Category: Transcriptional regulator]]
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Current revision

Structure of truncated CcpA in complex with P-Ser-HPr and Sulfate ions

PDB ID 2fep

Drag the structure with the mouse to rotate

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