Structural and Functional Insights into the Unwinding Mechanism of Bacteroides sp Pif1.
作者： Xianglian Zhou , Wendan Ren , Sakshibeedu R. Bharath , Xuhua Tang , Yang He
DOI: 10.1016/J.CELREP.2016.02.008
关键词:
摘要: Pif1 is a conserved SF1B DNA helicase involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. Here, we report the structures of domain human Bacteroides sp (BaPif1) complex with ADP-AlF4(-) two different single-stranded (ssDNAs). The wedge region equivalent to β hairpin other helicases folds into an extended loop followed by α helix. signature motif BaPif1 interacts short helix order stabilize these ssDNA binding elements, therefore indirectly exerting its functional role. Domain 2B undergoes large conformational change upon concomitant ATP ssDNA, which critical for Pif1's activities. cocrystallized tailed dsDNA ADP-AlF4(-), resulting bound bent nearly 90° at ssDNA/dsDNA junction. snapshots provide insights mechanism governing activity Pif1.
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