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- W2110943589 abstract "Within minutes after infecting Escherichia coli, bacteriophage T7 synthesizes many copies of its genomic DNA. The lynchpin of the T7 replication system is a bifunctional primase-helicase that unwinds duplex DNA at the replication fork while initiating the synthesis of Okazaki fragments on the lagging strand. We have determined a 3.45 A crystal structure of the T7 primase-helicase that shows an articulated arrangement of the primase and helicase sites. The crystallized primase-helicase is a heptamer with a crown-like shape, reflecting an intimate packing of helicase domains into a ring that is topped with loosely arrayed primase domains. This heptameric isoform can accommodate double-stranded DNA in its central channel, which nicely explains its recently described DNA remodeling activity. The double-jointed structure of the primase-helicase permits a free range of motion for the primase and helicase domains that suggests how the continuous unwinding of DNA at the replication fork can be periodically coupled to Okazaki fragment synthesis." @default.
- W2110943589 created "2016-06-24" @default.
- W2110943589 creator A5016221669 @default.
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- W2110943589 creator A5053075000 @default.
- W2110943589 creator A5056306966 @default.
- W2110943589 creator A5060002817 @default.
- W2110943589 date "2003-11-01" @default.
- W2110943589 modified "2023-09-28" @default.
- W2110943589 title "The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7" @default.
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- W2110943589 doi "https://doi.org/10.1016/s1097-2765(03)00442-8" @default.
- W2110943589 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14636571" @default.
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