4r94

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

spinqualitylabelsall models 4r94, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r94 is a 1 chain structure with sequence from Murine minute virus strain MVM prototype. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.668Å Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NS1_MUMIP Multifunctional protein that plays an essential role in viral DNA replication. Inhibits the host cell cycle during the G1/S transition, the S-phase, and the G2/M transition. These arrests may provide essential cellular factors for viral DNA replication. Interacts specifically with the viral DNA origin of replication and plays a direct role in DNA replication. Participates in the transcriptional regulation of several promoters including the viral p38 promoter that regulates the expression of VP1 and VP2 transcripts. Promotes apoptosis in host cell. Publication Abstract from PubMed 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 1.45A 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. Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding.,Tewary SK, Liang L, Lin Z, Lynn A, Cotmore SF, Tattersall P, Zhao H, Tang L Virology. 2014 Dec 17;476C:61-71. doi: 10.1016/j.virol.2014.11.022. PMID:25528417 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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