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- W2980497632 startingPage "e0223875" @default.
- W2980497632 abstract "Several pathways exist to bypass DNA damage during replication. One such pathway is template switching. The Rad5 protein plays two important roles in template switching: it is an E3 ubiquitin ligase that catalyzes PCNA poly-ubiquitylation and it is a helicase that converts replication forks to chicken foot structures. To understand the structure, conformational flexibility, and mechanism of Rad5, we used a full-ensemble hybrid method combining Langevin dynamics simulations and small-angle X-ray scattering. From these studies, we generated the first experimentally validated, high-resolution structural model of Rad5. We found that Rad5 is more compact and less extended than is suggested by its large amount of predicted intrinsic disorder. Thus, Rad5 likely has a novel intra-molecular interaction that limits the range of conformational space it can sample. We provide evidence for a novel interaction between the HIRAN and the helicase domains of Rad5, and we discuss the biological and mechanistic implications of this." @default.
- W2980497632 created "2019-10-25" @default.
- W2980497632 creator A5073752419 @default.
- W2980497632 creator A5079313612 @default.
- W2980497632 date "2019-10-18" @default.
- W2980497632 modified "2023-10-16" @default.
- W2980497632 title "Conformational flexibility of fork-remodeling helicase Rad5 shown by full-ensemble hybrid methods" @default.
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- W2980497632 doi "https://doi.org/10.1371/journal.pone.0223875" @default.
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