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| | <StructureSection load='4wls' size='340' side='right'caption='[[4wls]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4wls' size='340' side='right'caption='[[4wls]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wls]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_dh5[alpha] Escherichia coli dh5[alpha]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WLS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WLS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wls]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH5alpha Escherichia coli DH5alpha] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WLS FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wlw|4wlw]]</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=4wls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wls OCA], [https://pdbe.org/4wls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wls RCSB], [https://www.ebi.ac.uk/pdbsum/4wls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wls ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cueR, ybbI, b0487, JW0476 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=668369 Escherichia coli DH5[alpha]])</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=4wls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wls OCA], [http://pdbe.org/4wls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wls RCSB], [http://www.ebi.ac.uk/pdbsum/4wls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wls ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CUER_ECOLI CUER_ECOLI]] Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.<ref>PMID:10915804</ref> <ref>PMID:11399769</ref> | + | [https://www.uniprot.org/uniprot/CUER_ECOLI CUER_ECOLI] Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.<ref>PMID:10915804</ref> <ref>PMID:11399769</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4wls" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4wls" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Canalizo-Hernandez, M]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Halloran, T V.O]] | + | [[Category: Canalizo-Hernandez M]] |
| - | [[Category: Mondragon, A]] | + | [[Category: Mondragon A]] |
| - | [[Category: Philips, S J]] | + | [[Category: O'Halloran TV]] |
| - | [[Category: Merr-family transcription regulator]] | + | [[Category: Philips SJ]] |
| - | [[Category: Metal-free form]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
| - | [[Category: Repressor]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulator-dna complex]]
| + | |
| Structural highlights
Function
CUER_ECOLI Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.[1] [2]
Publication Abstract from PubMed
Many transcriptional activators act at a distance from core promoter elements and work by recruiting RNA polymerase through protein-protein interactions. We show here how the prokaryotic regulatory protein CueR both represses and activates transcription by differentially modulating local DNA structure within the promoter. Structural studies reveal that the repressor state slightly bends the promoter DNA, precluding optimal RNA polymerase-promoter recognition. Upon binding a metal ion in the allosteric site, CueR switches into an activator conformation. It maintains all protein-DNA contacts but introduces torsional stresses that kink and undertwist the promoter, stabilizing an A-form DNA-like conformation. These factors switch on and off transcription by exerting dynamic control of DNA stereochemistry, reshaping the core promoter and making it a better or worse substrate for polymerase.
TRANSCRIPTION. Allosteric transcriptional regulation via changes in the overall topology of the core promoter.,Philips SJ, Canalizo-Hernandez M, Yildirim I, Schatz GC, Mondragon A, O'Halloran TV Science. 2015 Aug 21;349(6250):877-81. doi: 10.1126/science.aaa9809. PMID:26293965[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Outten FW, Outten CE, Hale J, O'Halloran TV. Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, cueR. J Biol Chem. 2000 Oct 6;275(40):31024-9. PMID:10915804 doi:http://dx.doi.org/10.1074/jbc.M006508200
- ↑ Outten FW, Huffman DL, Hale JA, O'Halloran TV. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem. 2001 Aug 17;276(33):30670-7. Epub 2001 Jun 8. PMID:11399769 doi:http://dx.doi.org/10.1074/jbc.M104122200
- ↑ Philips SJ, Canalizo-Hernandez M, Yildirim I, Schatz GC, Mondragon A, O'Halloran TV. TRANSCRIPTION. Allosteric transcriptional regulation via changes in the overall topology of the core promoter. Science. 2015 Aug 21;349(6250):877-81. doi: 10.1126/science.aaa9809. PMID:26293965 doi:http://dx.doi.org/10.1126/science.aaa9809
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