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Structures of minute virus of mice replication initiator protein N-terminal domain: insights into DNA nicking and origin binding
dc.contributor.author | Tewary, Sunil Kumar | |
dc.contributor.author | Liang, Lingfei | |
dc.contributor.author | Lin, Zihan | |
dc.contributor.author | Lynn, Anna Y. | |
dc.contributor.author | Cotmore, Susan F. | |
dc.contributor.author | Tattersall, Peter | |
dc.contributor.author | Zhao, Haiyan | |
dc.contributor.author | Tang, Liang | |
dc.date.accessioned | 2016-02-12T21:47:40Z | |
dc.date.available | 2016-02-12T21:47:40Z | |
dc.date.issued | 2016-02-01 | |
dc.identifier.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 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/20073 | |
dc.description | This is the author's accepted manuscript. The original is available at http://www.sciencedirect.com/science/article/pii/S0042682214005236 | en_US |
dc.description.abstract | 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. | en_US |
dc.publisher | Elsevier | en_US |
dc.subject | Parvovirus | en_US |
dc.subject | DNA replication | en_US |
dc.subject | Non-structural protein 1 | en_US |
dc.subject | Site-specific DNA binding | en_US |
dc.subject | Nickase | en_US |
dc.subject | Nuclease | en_US |
dc.title | Structures of minute virus of mice replication initiator protein N-terminal domain: insights into DNA nicking and origin binding | en_US |
dc.type | Article | |
kusw.kuauthor | Tang, Liang | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1016/j.virol.2014.11.022 | |
dc.identifier.orcid | https://orcid.org/0000-0002-2659-3284 https://orcid.org/0000-0001-5812-1866 | |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |