7UDI

Full-length dimer of DNA-Damage Response Protein C from Deinococcus radiodurans

7UDI の概要

• エントリーDOI: 10.2210/pdb7udi/pdb
• 分子名称: DNA damage response protein DdrC, SULFATE ION (3 entities in total)
• 機能のキーワード: dna repair, radioresistance, dna binding protein
• 由来する生物種: Deinococcus radiodurans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51200.19

構造登録者

Szabla, R.,Li, M.C.,Junop, M.S. (登録日: 2022-03-19, 公開日: 2023-02-22, 最終更新日: 2024-10-23)

主引用文献

Szabla, R.,Li, M.,Warner, V.,Song, Y.,Junop, M.
DdrC, a unique DNA repair factor from D. radiodurans, senses and stabilizes DNA breaks through a novel lesion-recognition mechanism.
Nucleic Acids Res., 2024

PubMed Abstract: The bacterium Deinococcus radiodurans is known to survive high doses of DNA damaging agents. This resistance is the result of robust antioxidant systems which protect efficient DNA repair mechanisms that are unique to Deinococcus species. The protein DdrC has been identified as an important component of this repair machinery. DdrC is known to bind to DNA in vitro and has been shown to circularize and compact DNA fragments. The mechanism and biological relevance of this activity is poorly understood. Here, we show that the DdrC homodimer is a lesion-sensing protein that binds to two single-strand (ss) or double-strand (ds) breaks. The immobilization of DNA breaks in pairs consequently leads to the circularization of linear DNA and the compaction of nicked DNA. The degree of compaction is directly proportional with the number of available nicks. Previously, the structure of the DdrC homodimer was solved in an unusual asymmetric conformation. Here, we solve the structure of DdrC under different crystallographic environments and confirm that the asymmetry is an endogenous feature of DdrC. We propose a dynamic structural mechanism where the asymmetry is necessary to trap a pair of lesions. We support this model with mutant disruption and computational modeling experiments.

PubMed: 39036966
DOI: 10.1093/nar/gkae635

実験手法

X-RAY DIFFRACTION (2.24 Å)