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| <StructureSection load='6ro6' size='340' side='right'caption='[[6ro6]], [[Resolution|resolution]] 1.41Å' scene=''> | | <StructureSection load='6ro6' size='340' side='right'caption='[[6ro6]], [[Resolution|resolution]] 1.41Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6ro6]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_17065 Dsm 17065]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RO6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ro6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_deserti Deinococcus deserti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RO6 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.41Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rnx|6rnx]], [[6rnz|6rnz]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ddrOC, Deide_20570 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=310783 DSM 17065])</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=6ro6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ro6 OCA], [https://pdbe.org/6ro6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ro6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ro6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ro6 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=6ro6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ro6 OCA], [http://pdbe.org/6ro6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ro6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ro6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ro6 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/DDROC_DEIDV DDROC_DEIDV]] Repressor specific for genes preceded by a radiation/desiccation response motif (RDRM) site, which is present upstream of several radiation-induced genes.<ref>PMID:25170972</ref> | + | [https://www.uniprot.org/uniprot/DDROC_DEIDV DDROC_DEIDV] Repressor specific for genes preceded by a radiation/desiccation response motif (RDRM) site, which is present upstream of several radiation-induced genes.<ref>PMID:25170972</ref> |
| <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: Dsm 17065]] | + | [[Category: Deinococcus deserti]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Arnoux, P]] | + | [[Category: Arnoux P]] |
- | [[Category: Blanchard, L]] | + | [[Category: Blanchard L]] |
- | [[Category: Brandelet, G]] | + | [[Category: Brandelet G]] |
- | [[Category: Groot, A De]] | + | [[Category: De Groot A]] |
- | [[Category: Pignol, D]] | + | [[Category: Pignol D]] |
- | [[Category: Siponen, M I]] | + | [[Category: Siponen MI]] |
- | [[Category: Dna binding protein]]
| + | |
| Structural highlights
Function
DDROC_DEIDV Repressor specific for genes preceded by a radiation/desiccation response motif (RDRM) site, which is present upstream of several radiation-induced genes.[1]
Publication Abstract from PubMed
Exposure to harmful conditions such as radiation and desiccation induce oxidative stress and DNA damage. In radiation-resistant Deinococcus bacteria, the radiation/desiccation response is controlled by two proteins: the XRE family transcriptional repressor DdrO and the COG2856 metalloprotease IrrE. The latter cleaves and inactivates DdrO. Here, we report the biochemical characterization and crystal structure of DdrO, which is the first structure of a XRE protein targeted by a COG2856 protein. DdrO is composed of two domains that fold independently and are separated by a flexible linker. The N-terminal domain corresponds to the DNA-binding domain. The C-terminal domain, containing three alpha helices arranged in a novel fold, is required for DdrO dimerization. Cleavage by IrrE occurs in the loop between the last two helices of DdrO and abolishes dimerization and DNA binding. The cleavage site is hidden in the DdrO dimer structure, indicating that IrrE cleaves DdrO monomers or that the interaction with IrrE induces a structural change rendering accessible the cleavage site. Predicted COG2856/XRE regulatory protein pairs are found in many bacteria, and available data suggest two different molecular mechanisms for stress-induced gene expression: COG2856 protein-mediated cleavage or inhibition of oligomerization without cleavage of the XRE repressor.
Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus.,de Groot A, Siponen MI, Magerand R, Eugenie N, Martin-Arevalillo R, Doloy J, Lemaire D, Brandelet G, Parcy F, Dumas R, Roche P, Servant P, Confalonieri F, Arnoux P, Pignol D, Blanchard L Nucleic Acids Res. 2019 Oct 10. pii: 5584639. doi: 10.1093/nar/gkz883. PMID:31598697[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ludanyi M, Blanchard L, Dulermo R, Brandelet G, Bellanger L, Pignol D, Lemaire D, de Groot A. Radiation response in Deinococcus deserti: IrrE is a metalloprotease that cleaves repressor protein DdrO. Mol Microbiol. 2014 Oct;94(2):434-49. doi: 10.1111/mmi.12774. Epub 2014 Sep 18. PMID:25170972 doi:http://dx.doi.org/10.1111/mmi.12774
- ↑ de Groot A, Siponen MI, Magerand R, Eugenie N, Martin-Arevalillo R, Doloy J, Lemaire D, Brandelet G, Parcy F, Dumas R, Roche P, Servant P, Confalonieri F, Arnoux P, Pignol D, Blanchard L. Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus. Nucleic Acids Res. 2019 Oct 10. pii: 5584639. doi: 10.1093/nar/gkz883. PMID:31598697 doi:http://dx.doi.org/10.1093/nar/gkz883
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