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6JQ1

Crystal Structure of DdrO from Deinococcus geothermalis

Summary for 6JQ1
Entry DOI10.2210/pdb6jq1/pdb
DescriptorTranscriptional regulator, XRE family, LITHIUM ION (3 entities in total)
Functional Keywordstranscription factor, xre, hth, dimerization, dna binding protein
Biological sourceDeinococcus geothermalis DSM 11300
Total number of polymer chains2
Total formula weight29896.66
Authors
Lu, H.,Hua, Y.,Zhao, Y. (deposition date: 2019-03-28, release date: 2019-08-28, Last modification date: 2023-11-22)
Primary citationLu, 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: 31410466
DOI: 10.1093/nar/gkz720
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

238895

數據於2025-07-16公開中

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