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- W4200461102 abstract "Two new structures of the N-terminal domain of the main replication protein, NS1, of Human Parvovirus B19 (B19V) are presented. This domain (NS1-nuc) plays an important role in the “rolling hairpin” replication of the single-stranded B19V DNA genome, recognizing origin of replication sequences in double-stranded DNA, and cleaving (i.e. nicking) single-stranded DNA at a nearby site known as the trs. One structure of NS1-nuc is solved to 2.4 Å and shows the positions of two bound phosphate ions. A second structure shows the position of a single divalent cation in the DNA nicking active site. The three-dimensional structure of NS1-nuc is well conserved between the two forms, as well as with a previously solved structure of a sequence variant of the same domain, however shown here at significantly higher resolution. Using structures of NS1-nuc homologues bound to single- and double-stranded DNA, models for DNA recognition and nicking by B19V NS1-nuc are presented which predict residues important for DNA cleavage and for sequence specific recognition at the viral origin of replication." @default.
- W4200461102 created "2021-12-31" @default.
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- W4200461102 date "2021-12-21" @default.
- W4200461102 modified "2023-10-15" @default.
- W4200461102 title "High-Resolution Structure of the Nuclease Domain of the Human Parvovirus B19 Main Replication Protein NS1" @default.
- W4200461102 doi "https://doi.org/10.1101/2021.12.20.473600" @default.
- W4200461102 hasPublicationYear "2021" @default.
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