2hsg: Difference between revisions
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<StructureSection load='2hsg' size='340' side='right'caption='[[2hsg]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2hsg' size='340' side='right'caption='[[2hsg]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hsg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2hsg]] is a 1 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=2HSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HSG 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]] 2.5Å</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=2hsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsg OCA], [https://pdbe.org/2hsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsg RCSB], [https://www.ebi.ac.uk/pdbsum/2hsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsg 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=2hsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsg OCA], [https://pdbe.org/2hsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsg RCSB], [https://www.ebi.ac.uk/pdbsum/2hsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsg ProSAT]</span></td></tr> | ||
</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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alings | [[Category: Priestia megaterium]] | ||
[[Category: Biesiadka | [[Category: Alings C]] | ||
[[Category: Loll | [[Category: Biesiadka J]] | ||
[[Category: Saenger | [[Category: Loll B]] | ||
[[Category: Saenger W]] | |||
Latest revision as of 13:01, 30 August 2023
Structure of transcription regulator CcpA in its DNA-free stateStructure of transcription regulator CcpA in its DNA-free state
Structural highlights
FunctionCCPA_PRIMG Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe catabolite control protein A (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR-LacI. CcpA functions as master transcriptional regulator of carbon catabolite repression/regulation in firmicutes. Here we present the crystal structure of full-length apo CcpA at 2.5 A resolution from B. megaterium. The structure reveals the location of the helix-turn-helix domain as well as the hinge region, which were not visible due to their high flexibility in earlier crystallographic studies on CcpA molecules. The structure of the apo CcpA homodimer in the present form is in contrast to other reported structures for CcpA. Structure of full-length transcription regulator CcpA in the apo form.,Loll B, Saenger W, Biesiadka J Biochim Biophys Acta. 2007 Jun;1774(6):732-6. Epub 2007 Apr 18. PMID:17500051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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