6S16

T. thermophilus RuvC in complex with Holliday junction substrate

6S16 の概要

• エントリーDOI: 10.2210/pdb6s16/pdb
• 分子名称: Crossover junction endodeoxyribonuclease RuvC, DNA (33-MER), DNA (5'-D(*AP*TP*CP*TP*GP*CP*CP*GP*AP*TP*TP*C)-3'), ... (6 entities in total)
• 機能のキーワード: ruvc resolvase holliday junction, hydrolase
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 66616.24

構造登録者

Gorecka, K.M.,Krepl, M.,Szlachcic, A.,Poznanski, J.,Sponer, J.,Nowotny, M. (登録日: 2019-06-18, 公開日: 2019-09-25, 最終更新日: 2024-01-24)

主引用文献

Gorecka, K.M.,Krepl, M.,Szlachcic, A.,Poznanski, J.,Sponer, J.,Nowotny, M.
RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution.
Nat Commun, 10:4102-4102, 2019

PubMed Abstract: Holliday junctions (HJs) are four-way DNA structures that occur in DNA repair by homologous recombination. Specialized nucleases, termed resolvases, remove (i.e., resolve) HJs. The bacterial protein RuvC is a canonical resolvase that introduces two symmetric cuts into the HJ. For complete resolution of the HJ, the two cuts need to be tightly coordinated. They are also specific for cognate DNA sequences. Using a combination of structural biology, biochemistry, and a computational approach, here we show that correct positioning of the substrate for cleavage requires conformational changes within the bound DNA. These changes involve rare high-energy states with protein-assisted base flipping that are readily accessible for the cognate DNA sequence but not for non-cognate sequences. These conformational changes and the relief of protein-induced structural tension of the DNA facilitate coordination between the two cuts. The unique DNA cleavage mechanism of RuvC demonstrates the importance of high-energy conformational states in nucleic acid readouts.

PubMed: 31506434
DOI: 10.1038/s41467-019-11900-8

実験手法

X-RAY DIFFRACTION (3.409 Å)