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| | <StructureSection load='1xhf' size='340' side='right'caption='[[1xhf]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='1xhf' size='340' side='right'caption='[[1xhf]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xhf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XHF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xhf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XHF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=BF2:BERYLLIUM+DIFLUORIDE'>BF2</scene>, <scene name='pdbligand=BF4:BERYLLIUM+TETRAFLUORIDE+ION'>BF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.152Å</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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=BF2:BERYLLIUM+DIFLUORIDE'>BF2</scene>, <scene name='pdbligand=BF4:BERYLLIUM+TETRAFLUORIDE+ION'>BF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xhe|1xhe]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">arcA, dye, fexA, sfrA, seg, msp, cpxC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1xhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xhf OCA], [https://pdbe.org/1xhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xhf RCSB], [https://www.ebi.ac.uk/pdbsum/1xhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xhf 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=1xhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xhf OCA], [https://pdbe.org/1xhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xhf RCSB], [https://www.ebi.ac.uk/pdbsum/1xhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xhf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ARCA_ECOLI ARCA_ECOLI]] Member of the two-component regulatory system ArcB/ArcA. Represses a wide variety of aerobic enzymes under anaerobic conditions. Controls the resistance of E.coli to dyes; required for expression of the alkaline phosphatase and sex factor F genes; It also may be involved in the osmoregulation of envelope proteins. When activated by ArcB, it negatively regulates the expression of genes of aerobic function. Activates the transcription of the plfB operon by binding to its promoter.
| + | [https://www.uniprot.org/uniprot/ARCA_ECOLI ARCA_ECOLI] Member of the two-component regulatory system ArcB/ArcA. Represses a wide variety of aerobic enzymes under anaerobic conditions. Controls the resistance of E.coli to dyes; required for expression of the alkaline phosphatase and sex factor F genes; It also may be involved in the osmoregulation of envelope proteins. When activated by ArcB, it negatively regulates the expression of genes of aerobic function. Activates the transcription of the plfB operon by binding to its promoter. |
| | == 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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mack, T R]] | + | [[Category: Mack TR]] |
| - | [[Category: Stock, A M]] | + | [[Category: Stock AM]] |
| - | [[Category: Toro-Roman, A]] | + | [[Category: Toro-Roman A]] |
| - | [[Category: Anoxic redox control]]
| + | |
| - | [[Category: Doubly wound five-stranded beta/alpha fold]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| - | [[Category: Two-component system]]
| + | |
| Structural highlights
1xhf is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.152Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ARCA_ECOLI Member of the two-component regulatory system ArcB/ArcA. Represses a wide variety of aerobic enzymes under anaerobic conditions. Controls the resistance of E.coli to dyes; required for expression of the alkaline phosphatase and sex factor F genes; It also may be involved in the osmoregulation of envelope proteins. When activated by ArcB, it negatively regulates the expression of genes of aerobic function. Activates the transcription of the plfB operon by binding to its promoter.
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 PubMed
Escherichia coli react to changes from aerobic to anaerobic conditions of growth using the ArcA-ArcB two-component signal transduction system. This system, in conjunction with other proteins, regulates the respiratory metabolic pathways in the organism. ArcA is a member of the OmpR/PhoB subfamily of response regulator transcription factors that are known to regulate transcription by binding in tandem to target DNA direct repeats. It is still unclear in this subfamily how activation by phosphorylation of the regulatory domain of response regulators stimulates DNA binding by the effector domain and how dimerization and domain orientation, as well as intra- and intermolecular interactions, affect this process. In order to address these questions we have solved the crystal structures of the regulatory domain of ArcA in the presence and absence of the phosphoryl analog, BeF3-. In the crystal structures, the regulatory domain of ArcA forms a symmetric dimer mediated by the alpha4-beta5-alpha5 face of the protein and involving a number of residues that are highly conserved in the OmpR/PhoB subfamily. It is hypothesized that members of this subfamily use a common mechanism of regulation by dimerization. Additional biophysical studies were employed to probe the oligomerization state of ArcA, as well as its individual domains, in solution. The solution studies show the propensity of the individual domains to associate into oligomers larger than the dimer observed for the intact protein, and suggest that the C-terminal DNA-binding domain also plays a role in oligomerization.
Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.,Toro-Roman A, Mack TR, Stock AM J Mol Biol. 2005 May 27;349(1):11-26. Epub 2005 Apr 7. PMID:15876365[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Toro-Roman A, Mack TR, Stock AM. Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face. J Mol Biol. 2005 May 27;349(1):11-26. Epub 2005 Apr 7. PMID:15876365 doi:10.1016/j.jmb.2005.03.059
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