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| | <StructureSection load='5lbm' size='340' side='right'caption='[[5lbm]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='5lbm' size='340' side='right'caption='[[5lbm]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lbm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LBM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LBM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lbm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LBM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</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]] 2.7Å</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">frmR, Z0457, ECs0412 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=5lbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbm OCA], [https://pdbe.org/5lbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lbm RCSB], [https://www.ebi.ac.uk/pdbsum/5lbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbm ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbm OCA], [http://pdbe.org/5lbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lbm RCSB], [http://www.ebi.ac.uk/pdbsum/5lbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FRMR_ECO57 FRMR_ECO57]] Repressor of the frmRAB operon. | + | [https://www.uniprot.org/uniprot/FRMR_ECO57 FRMR_ECO57] Repressor of the frmRAB operon. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco57]] | + | [[Category: Escherichia coli O157:H7]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baker, P J]] | + | [[Category: Baker PJ]] |
| - | [[Category: Bisson, C]] | + | [[Category: Bisson C]] |
| - | [[Category: Chivers, P T]] | + | [[Category: Chivers PT]] |
| - | [[Category: Green, J]] | + | [[Category: Green J]] |
| - | [[Category: Csor/rcnr escherichia coli frmr methylene bridge]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
FRMR_ECO57 Repressor of the frmRAB operon.
Publication Abstract from PubMed
Most organisms are exposed to the genotoxic chemical formaldehyde, either from endogenous or environmental sources. Therefore, biology has evolved systems to perceive and detoxify formaldehyde. The frmRA(B) operon that is present in many bacteria represents one such system. The FrmR protein is a transcriptional repressor that is specifically inactivated in the presence of formaldehyde, permitting expression of the formaldehyde detoxification machinery (FrmA and FrmB, when the latter is present). The X-ray structure of the formaldehyde-treated Escherichia coli FrmR (EcFrmR) protein reveals the formation of methylene bridges that link adjacent Pro2 and Cys35 residues in the EcFrmR tetramer. Methylene bridge formation has profound effects on the pattern of surface charge of EcFrmR and combined with biochemical/biophysical data suggests a mechanistic model for formaldehyde-sensing and derepression of frmRA(B) expression in numerous bacterial species.
The mechanism of a formaldehyde-sensing transcriptional regulator.,Denby KJ, Iwig J, Bisson C, Westwood J, Rolfe MD, Sedelnikova SE, Higgins K, Maroney MJ, Baker PJ, Chivers PT, Green J Sci Rep. 2016 Dec 9;6:38879. doi: 10.1038/srep38879. PMID:27934966[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Denby KJ, Iwig J, Bisson C, Westwood J, Rolfe MD, Sedelnikova SE, Higgins K, Maroney MJ, Baker PJ, Chivers PT, Green J. The mechanism of a formaldehyde-sensing transcriptional regulator. Sci Rep. 2016 Dec 9;6:38879. doi: 10.1038/srep38879. PMID:27934966 doi:http://dx.doi.org/10.1038/srep38879
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