6JQ1

Crystal Structure of DdrO from Deinococcus geothermalis

6JQ1 の概要

• エントリーDOI: 10.2210/pdb6jq1/pdb
• 分子名称: Transcriptional regulator, XRE family, LITHIUM ION (3 entities in total)
• 機能のキーワード: transcription factor, xre, hth, dimerization, dna binding protein
• 由来する生物種: Deinococcus geothermalis DSM 11300
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29896.66

構造登録者

Lu, H.,Hua, Y.,Zhao, Y. (登録日: 2019-03-28, 公開日: 2019-08-28, 最終更新日: 2023-11-22)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.3 Å)