4R94

Structure of the nickase domain of NS1 from MVM complexed with magnesium

Summary for 4R94

• Entry DOI: 10.2210/pdb4r94/pdb
• Related: 3WRN 4PP4
• Descriptor: Non-structural protein NS1, MAGNESIUM ION (3 entities in total)
• Functional Keywords: nickase domain, dna binding, magnesium, nickase, replication
• Biological source: Murine minute virus (MVM)
• Total number of polymer chains: 1
• Total formula weight: 30065.16

Authors

Liang, L.,Zhao, H.,Tang, L. (deposition date: 2014-09-03, release date: 2015-01-21, Last modification date: 2023-11-08)

Primary citation

Tewary, S.K.,Liang, L.,Lin, Z.,Lynn, A.,Cotmore, S.F.,Tattersall, P.,Zhao, H.,Tang, L.
Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding.
Virology, 476C:61-71, 2014

PubMed 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 1.45Å 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.

PubMed: 25528417
DOI: 10.1016/j.virol.2014.11.022

Experimental method

X-RAY DIFFRACTION (1.668 Å)