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| <StructureSection load='4p9f' size='340' side='right'caption='[[4p9f]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4p9f' size='340' side='right'caption='[[4p9f]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4p9f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_umea_3718-1 Escherichia coli umea 3718-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P9F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p9f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UMEA_3718-1 Escherichia coli UMEA 3718-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P9F 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.099Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">G994_01403 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1281269 Escherichia coli UMEA 3718-1])</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='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=4p9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9f OCA], [http://pdbe.org/4p9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p9f RCSB], [http://www.ebi.ac.uk/pdbsum/4p9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p9f 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=4p9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9f OCA], [https://pdbe.org/4p9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p9f RCSB], [https://www.ebi.ac.uk/pdbsum/4p9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p9f ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| </div> | | </div> |
| <div class="pdbe-citations 4p9f" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4p9f" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Escherichia coli umea 3718-1]] | + | [[Category: Escherichia coli UMEA 3718-1]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Lord, D M]] | + | [[Category: Lord DM]] |
- | [[Category: Page, R]] | + | [[Category: Page R]] |
- | [[Category: Peti, W]] | + | [[Category: Peti W]] |
- | [[Category: Biofilm formation]]
| + | |
- | [[Category: Gntr family]]
| + | |
- | [[Category: Transcription]]
| + | |
- | [[Category: Transcriptional regulator]]
| + | |
| Structural highlights
Publication Abstract from PubMed
MqsR-controlled colanic acid and biofilm regulator (McbR, also known as YncC) is the protein product of a highly induced gene in early Escherichia coli biofilm development and has been regarded as an attractive target for blocking biofilm formation. This protein acts as a repressor for genes involved in exopolysaccharide production and an activator for genes involved in stress response. To better understand the role of McbR in governing the switch from exponential growth to the biofilm state, we determined the crystal structure of McbR to 2.1 A. The structure reveals McbR to be a member of the FadR C-terminal domain (FCD) family of the GntR superfamily of transcriptional regulators (this family was named after the first identified member, GntR, a transcriptional repressor of the gluconate operon of Bacillus subtilis). Previous to this study, only six of the predicted 2800 members of this family had been structurally characterized. Here, we identify the residues that constitute the McbR effector and DNA binding sites. In addition, comparison of McbR with other members of the FCD domain family shows that this family of proteins adopts highly distinct oligomerization interfaces, which has implications for DNA binding and regulation.
McbR/YncC: implications for the mechanism of ligand and DNA binding by a bacterial GntR transcriptional regulator involved in biofilm formation.,Lord DM, Uzgoren Baran A, Soo VW, Wood TK, Peti W, Page R Biochemistry. 2014 Nov 25;53(46):7223-31. doi: 10.1021/bi500871a. Epub 2014 Nov, 7. PMID:25376905[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lord DM, Uzgoren Baran A, Soo VW, Wood TK, Peti W, Page R. McbR/YncC: implications for the mechanism of ligand and DNA binding by a bacterial GntR transcriptional regulator involved in biofilm formation. Biochemistry. 2014 Nov 25;53(46):7223-31. doi: 10.1021/bi500871a. Epub 2014 Nov, 7. PMID:25376905 doi:http://dx.doi.org/10.1021/bi500871a
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