6RNX

Crystal structure of the essential repressor DdrO from radiation-resistant Deinococcus bacteria (Deinococcus deserti)

6RNX の概要

• エントリーDOI: 10.2210/pdb6rnx/pdb
• 関連するPDBエントリー: 6RMQ
• 分子名称: HTH-type transcriptional regulator DdrOC, CHLORIDE ION (3 entities in total)
• 機能のキーワード: dna binding protein
• 由来する生物種: Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29553.17

構造登録者

Arnoux, P.,Siponen, M.I.,Pignol, D.,De Groot, A.,Blanchard, L. (登録日: 2019-05-09, 公開日: 2019-10-09, 最終更新日: 2024-01-24)

主引用文献

de Groot, A.,Siponen, M.I.,Magerand, R.,Eugenie, N.,Martin-Arevalillo, R.,Doloy, J.,Lemaire, D.,Brandelet, G.,Parcy, F.,Dumas, R.,Roche, P.,Servant, P.,Confalonieri, F.,Arnoux, P.,Pignol, D.,Blanchard, L.
Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus.
Nucleic Acids Res., 47:11403-11417, 2019

PubMed Abstract: Exposure to harmful conditions such as radiation and desiccation induce oxidative stress and DNA damage. In radiation-resistant Deinococcus bacteria, the radiation/desiccation response is controlled by two proteins: the XRE family transcriptional repressor DdrO and the COG2856 metalloprotease IrrE. The latter cleaves and inactivates DdrO. Here, we report the biochemical characterization and crystal structure of DdrO, which is the first structure of a XRE protein targeted by a COG2856 protein. DdrO is composed of two domains that fold independently and are separated by a flexible linker. The N-terminal domain corresponds to the DNA-binding domain. The C-terminal domain, containing three alpha helices arranged in a novel fold, is required for DdrO dimerization. Cleavage by IrrE occurs in the loop between the last two helices of DdrO and abolishes dimerization and DNA binding. The cleavage site is hidden in the DdrO dimer structure, indicating that IrrE cleaves DdrO monomers or that the interaction with IrrE induces a structural change rendering accessible the cleavage site. Predicted COG2856/XRE regulatory protein pairs are found in many bacteria, and available data suggest two different molecular mechanisms for stress-induced gene expression: COG2856 protein-mediated cleavage or inhibition of oligomerization without cleavage of the XRE repressor.

PubMed: 31598697
DOI: 10.1093/nar/gkz883

実験手法

X-RAY DIFFRACTION (2.84 Å)