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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Detalles Bibliográficos
Autores principales: Li, Na, Shi, Ke, Rao, Timsi, Banerjee, Surajit, Aihara, Hideki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6962361/
https://www.ncbi.nlm.nih.gov/pubmed/31941902
http://dx.doi.org/10.1038/s41598-019-56825-w

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6962361/
https://www.ncbi.nlm.nih.gov/pubmed/31941902
http://dx.doi.org/10.1038/s41598-019-56825-w

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