6JQ1
Crystal Structure of DdrO from Deinococcus geothermalis
Summary for 6JQ1
Entry DOI | 10.2210/pdb6jq1/pdb |
Descriptor | Transcriptional regulator, XRE family, LITHIUM ION (3 entities in total) |
Functional Keywords | transcription factor, xre, hth, dimerization, dna binding protein |
Biological source | Deinococcus geothermalis DSM 11300 |
Total number of polymer chains | 2 |
Total formula weight | 29896.66 |
Authors | |
Primary citation | 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., 47:9925-9933, 2019 Cited by PubMed Abstract: 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 α-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. PubMed: 31410466DOI: 10.1093/nar/gkz720 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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