Structures of minute virus of mice replication initiator protein N-terminal domain: insights into DNA nicking and origin binding
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Issue Date
2016-02-01Author
Tewary, Sunil Kumar
Liang, Lingfei
Lin, Zihan
Lynn, Anna Y.
Cotmore, Susan F.
Tattersall, Peter
Zhao, Haiyan
Tang, Liang
Publisher
Elsevier
Type
Article
Article Version
Scholarly/refereed, author accepted manuscript
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Show full item recordAbstract
Members of the Parvoviridae family all encode a non-structural protein 1 (NS1) that directs replication of single-stranded viral DNA, packages viral DNA into capsid, and serves as a potent transcriptional activator. Here we report the X-ray structure of the minute virus of mice (MVM) NS1 N-terminal domain at 1.45 Å resolution, showing that sites for dsDNA binding, ssDNA binding and cleavage, nuclear localization, and other functions are integrated on a canonical fold of the histidine-hydrophobic-histidine superfamily of nucleases, including elements specific for this Protoparvovirus but distinct from its Bocaparvovirus or Dependoparvovirus orthologs. High resolution structural analysis reveals a nickase active site with an architecture that allows highly versatile metal ligand binding. The structures support a unified mechanism of replication origin recognition for homotelomeric and heterotelomeric parvoviruses, mediated by a basic-residue-rich hairpin and an adjacent helix in the initiator proteins and by tandem tetranucleotide motifs in the replication origins.
Description
This is the author's accepted manuscript. The original is available at http://www.sciencedirect.com/science/article/pii/S0042682214005236
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Citation
Tewary, Sunil K., Lingfei Liang, Zihan Lin, Annie Lynn, Susan F. Cotmore, Peter Tattersall, Haiyan Zhao, and Liang Tang. "Structures of Minute Virus of Mice Replication Initiator Protein N-terminal Domain: Insights into DNA Nicking and Origin Binding." Virology 476 (2015): 61-71. http://dx.doi.org/10.1016/j.virol.2014.11.022
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