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| | <StructureSection load='6jq1' size='340' side='right'caption='[[6jq1]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='6jq1' size='340' side='right'caption='[[6jq1]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jq1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Deigd Deigd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JQ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jq1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_geothermalis_DSM_11300 Deinococcus geothermalis DSM 11300]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JQ1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LI:LITHIUM+ION'>LI</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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dgeo_0336 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=319795 DEIGD])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI:LITHIUM+ION'>LI</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=6jq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jq1 OCA], [http://pdbe.org/6jq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jq1 RCSB], [http://www.ebi.ac.uk/pdbsum/6jq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jq1 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=6jq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jq1 OCA], [https://pdbe.org/6jq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jq1 RCSB], [https://www.ebi.ac.uk/pdbsum/6jq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jq1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q1J1J5_DEIGD Q1J1J5_DEIGD] |
| | <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: Deigd]] | + | [[Category: Deinococcus geothermalis DSM 11300]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hua, Y]] | + | [[Category: Hua Y]] |
| - | [[Category: Lu, H]] | + | [[Category: Lu H]] |
| - | [[Category: Zhao, Y]] | + | [[Category: Zhao Y]] |
| - | [[Category: Dimerization]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Hth]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| - | [[Category: Xre]]
| + | |
| Structural highlights
Function
Q1J1J5_DEIGD
Publication Abstract from PubMed
DdrO is an XRE family transcription repressor that, in coordination with the metalloprotease PprI, is critical in the DNA damage response of Deinococcus species. Here, we report the crystal structure of Deinococcus geothermalis DdrO. Biochemical and structural studies revealed the conserved recognizing alpha-helix and extended dimeric interaction of the DdrO protein, which are essential for promoter DNA binding. Two conserved oppositely charged residues in the HTH motif of XRE family proteins form salt bridge interactions that are essential for promoter DNA binding. Notably, the C-terminal domain is stabilized by hydrophobic interactions of leucine/isoleucine-rich helices, which is critical for DdrO dimerization. Our findings suggest that DdrO is a novel XRE family transcriptional regulator that forms a distinctive dimer. The structure also provides insight into the mechanism of DdrO-PprI-mediated DNA damage response in Deinococcus.
Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO.,Lu H, Wang L, Li S, Pan C, Cheng K, Luo Y, Xu H, Tian B, Zhao Y, Hua Y Nucleic Acids Res. 2019 Aug 14. pii: 5549711. doi: 10.1093/nar/gkz720. PMID:31410466[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu H, Wang L, Li S, Pan C, Cheng K, Luo Y, Xu H, Tian B, Zhao Y, Hua Y. Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO. Nucleic Acids Res. 2019 Aug 14. pii: 5549711. doi: 10.1093/nar/gkz720. PMID:31410466 doi:http://dx.doi.org/10.1093/nar/gkz720
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