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6S16

T. thermophilus RuvC in complex with Holliday junction substrate

Summary for 6S16
Entry DOI10.2210/pdb6s16/pdb
DescriptorCrossover 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)
Functional Keywordsruvc resolvase holliday junction, hydrolase
Biological sourceThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
More
Total number of polymer chains5
Total formula weight66616.24
Authors
Gorecka, K.M.,Krepl, M.,Szlachcic, A.,Poznanski, J.,Sponer, J.,Nowotny, M. (deposition date: 2019-06-18, release date: 2019-09-25, Last modification date: 2024-01-24)
Primary citationGorecka, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.409 Å)
Structure validation

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