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| | ==structure of ccpa-hpr-ser46p-ackA2 complex== | | ==structure of ccpa-hpr-ser46p-ackA2 complex== |
| - | <StructureSection load='3oqm' size='340' side='right' caption='[[3oqm]], [[Resolution|resolution]] 2.96Å' scene=''> | + | <StructureSection load='3oqm' size='340' side='right'caption='[[3oqm]], [[Resolution|resolution]] 2.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oqm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OQM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3oqm]] is a 6 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=3OQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OQM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.96Å</td></tr> |
| - | <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> | + | <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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oqn|3oqn]], [[3oqo|3oqo]]</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=3oqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oqm OCA], [https://pdbe.org/3oqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oqm RCSB], [https://www.ebi.ac.uk/pdbsum/3oqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oqm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alsA, amyR, BSU29740, ccpA, graR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]), BSU13900, hpr, ptsH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oqm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oqm RCSB], [http://www.ebi.ac.uk/pdbsum/3oqm PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3oqm" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Catabolite control protein|Catabolite control protein]] | + | *[[Catabolite control protein 3D structures|Catabolite control protein 3D structures]] |
| - | *[[Phosphocarrier protein HPr|Phosphocarrier protein HPr]] | + | *[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
| - | [[Category: Bartholomae, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Brennan, R G]] | + | [[Category: Bartholomae M]] |
| - | [[Category: Hillen, W]] | + | [[Category: Brennan RG]] |
| - | [[Category: Schumacher, M A]] | + | [[Category: Hillen W]] |
| - | [[Category: Sprehe, M]] | + | [[Category: Schumacher MA]] |
| - | [[Category: Hpr-ser46-p and cre dna]]
| + | [[Category: Sprehe M]] |
| - | [[Category: Nucleoid]]
| + | |
| - | [[Category: Pbp fold for ccpa]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription-transferase-dna complex]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
In Gram-positive bacteria, carbon catabolite protein A (CcpA) is the master regulator of carbon catabolite control, which ensures optimal energy usage under diverse conditions. Unlike other LacI-GalR proteins, CcpA is activated for DNA binding by first forming a complex with the phosphoprotein HPr-Ser46-P. Bacillus subtilis CcpA functions as both a transcription repressor and activator and binds to more than 50 operators called catabolite response elements (cres). These sites are highly degenerate with the consensus, WTGNNARCGNWWWCAW. How CcpA-(HPr-Ser46-P) binds such diverse sequences is unclear. To gain insight into this question, we solved the structures of the CcpA-(HPr-Ser46-P) complex bound to three different operators, the synthetic (syn) cre, ackA2 cre and gntR-down cre. Strikingly, the structures show that the CcpA-bound operators display different bend angles, ranging from 31 degrees to 56 degrees . These differences are accommodated by a flexible linkage between the CcpA helix-turn-helix-loop-helix motif and hinge helices, which allows independent docking of these DNA-binding modules. This flexibility coupled with an abundance of non-polar residues capable of non-specific nucleobase interactions permits CcpA-(HPr-Ser46-P) to bind diverse operators. Indeed, biochemical data show that CcpA-(HPr-Ser46-P) binds the three cre sites with similar affinities. Thus, the data reveal properties that license this protein to function as a global transcription regulator.
Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators.,Schumacher MA, Sprehe M, Bartholomae M, Hillen W, Brennan RG Nucleic Acids Res. 2010 Nov 23. PMID:21106498[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Henkin TM, Grundy FJ, Nicholson WL, Chambliss GH. Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and galR repressors. Mol Microbiol. 1991 Mar;5(3):575-84. PMID:1904524
- ↑ Kim JH, Guvener ZT, Cho JY, Chung KC, Chambliss GH. Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA. J Bacteriol. 1995 Sep;177(17):5129-34. PMID:7665492
- ↑ Tobisch S, Zuhlke D, Bernhardt J, Stulke J, Hecker M. Role of CcpA in regulation of the central pathways of carbon catabolism in Bacillus subtilis. J Bacteriol. 1999 Nov;181(22):6996-7004. PMID:10559165
- ↑ Ludwig H, Stulke J. The Bacillus subtilis catabolite control protein CcpA exerts all its regulatory functions by DNA-binding. FEMS Microbiol Lett. 2001 Sep 11;203(1):125-9. PMID:11557150
- ↑ Schumacher MA, Sprehe M, Bartholomae M, Hillen W, Brennan RG. Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators. Nucleic Acids Res. 2010 Nov 23. PMID:21106498 doi:10.1093/nar/gkq1177
- ↑ Schumacher MA, Sprehe M, Bartholomae M, Hillen W, Brennan RG. Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators. Nucleic Acids Res. 2010 Nov 23. PMID:21106498 doi:10.1093/nar/gkq1177
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