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| | ==Crystal structure of receiver domain of KdpE D52A mutant from E. coli== | | ==Crystal structure of receiver domain of KdpE D52A mutant from E. coli== |
| - | <StructureSection load='4l85' size='340' side='right' caption='[[4l85]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4l85' size='340' side='right'caption='[[4l85]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4l85]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L85 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l85]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L85 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0694, JW5096, kdpE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4l85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l85 OCA], [https://pdbe.org/4l85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l85 RCSB], [https://www.ebi.ac.uk/pdbsum/4l85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l85 ProSAT]</span></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=4l85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l85 OCA], [http://pdbe.org/4l85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l85 RCSB], [http://www.ebi.ac.uk/pdbsum/4l85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l85 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KDPE_ECOLI KDPE_ECOLI]] Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. | + | [https://www.uniprot.org/uniprot/KDPE_ECOLI KDPE_ECOLI] Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp 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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Kumar, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Yernool, D A]] | + | [[Category: Kumar S]] |
| - | [[Category: Receiver domain]] | + | [[Category: Yernool DA]] |
| - | [[Category: Transcription]]
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| Structural highlights
Function
KDPE_ECOLI Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon.
Publication Abstract from PubMed
Two-component signal transduction systems consist of pairs of histidine kinases and response regulators, which mediate adaptive responses to environmental cues. Most activated response regulators regulate transcription by binding tightly to promoter DNA via a phosphorylation-triggered inactive-to-active transition. The molecular basis for formation of stable response regulator-DNA complexes that precede the assembly of RNA polymerases is unclear. Here, we present structures of DNA complexed with the response regulator KdpE, a member of the OmpR/PhoB family. The distinctively asymmetric complex in an active-like conformation reveals a unique intramolecular interface between the receiver domain (RD) and the DNA-binding domain (DBD) of only one of the two response regulators in the complex. Structure-function studies show that this RD-DBD interface is necessary to form stable complexes that support gene expression. The conservation of sequence and structure suggests that these findings extend to a large group of response regulators that act as transcription factors.
An asymmetric heterodomain interface stabilizes a response regulator-DNA complex.,Narayanan A, Kumar S, Evrard AN, Paul LN, Yernool DA Nat Commun. 2014 Feb 14;5:3282. doi: 10.1038/ncomms4282. PMID:24526190[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Narayanan A, Kumar S, Evrard AN, Paul LN, Yernool DA. An asymmetric heterodomain interface stabilizes a response regulator-DNA complex. Nat Commun. 2014 Feb 14;5:3282. doi: 10.1038/ncomms4282. PMID:24526190 doi:http://dx.doi.org/10.1038/ncomms4282
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