View source for 6jq1


==Crystal Structure of DdrO from Deinococcus geothermalis==
<StructureSection load='6jq1' size='340' side='right'caption='[[6jq1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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'>[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>
== Function ==
[https://www.uniprot.org/uniprot/Q1J1J5_DEIGD Q1J1J5_DEIGD] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:31410466</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jq1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Deinococcus geothermalis DSM 11300]]
[[Category: Large Structures]]
[[Category: Hua Y]]
[[Category: Lu H]]
[[Category: Zhao Y]]