9GXT

C. thermocellum UvrA in complex with DNA with a fluorescein modification and AMPPNP (ATP-bound conformation 1)

9GXT の概要

• エントリーDOI: 10.2210/pdb9gxt/pdb
• EMDBエントリー: 51674
• 分子名称: UvrABC system protein A, DNA (50-MER) with a fluorescein modification - (random sequence built in model), ZINC ION, ... (4 entities in total)
• 機能のキーワード: dna binding protein, dna repair pathway, nucleotide excision repair pathway, ner
• 由来する生物種: Acetivibrio thermocellus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 247268.92

構造登録者

Nirwal, S.,Czarnocki-Cieciura, M.,Nowotny, M. (登録日: 2024-09-30, 公開日: 2025-12-24, 最終更新日: 2026-01-21)

主引用文献

Nirwal, S.,Czarnocki-Cieciura, M.,Zajko, W.,Skowronek, K.,Szczepanowski, R.H.,Nowotny, M.
Structural snapshots of the mechanism of ATP-dependent DNA damage recognition by UvrA.
Nat Commun, 17:387-387, 2025

PubMed Abstract: Nucleotide excision repair is a DNA repair pathway which detects and fixes various DNA lesions that distort the structure of DNA. In bacteria, the pathway starts with the UvrA protein which has two adenosine triphosphatase modules and forms dimers. The DNA is handed over from UvrA to UvrB, which is a weak helicase that verifies the presence of damage. Despite intense studies, the role of the ATPase activity of UvrA in damage recognition is unclear. Here, we present a series of cryo-electron microscopy structures of UvrA in complex with three different DNAs and in the presence and absence of nucleotides. We also present a structure of UvrA:UvrB:DNA complex. These structures reveal a major rearrangement of the UvrA dimer upon ATP binding. We propose that these conformational changes are used to mechanically probe the integrity of DNA for damage localization. Collectively, our results present snapshots of UvrA's ATP-dependent DNA damage detection.

PubMed: 41381534
DOI: 10.1038/s41467-025-67075-y

実験手法

ELECTRON MICROSCOPY (3.1 Å)