6jq1

Crystal Structure of DdrO from Deinococcus geothermalis

spinqualitylabelsall models 6jq1, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jq1 is a 2 chain structure with sequence from Deinococcus geothermalis DSM 11300. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: LI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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