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Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase

Fowlpox virus resolvase (Fpr) is an endonuclease that cleaves a broad range of branched DNA structures, including the Holliday junction (HJ), with little sequence-specificity. To better understand the mechanisms underlying its relaxed substrate specificity, we determined the crystal structures of Fp...

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Bibliografische gegevens
Gepubliceerd in:Sci Rep
Hoofdauteurs: Li, Na, Shi, Ke, Rao, Timsi, Banerjee, Surajit, Aihara, Hideki
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Nature Publishing Group UK 2020
Onderwerpen:
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC6962361/
https://ncbi.nlm.nih.gov/pubmed/31941902
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-019-56825-w
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