3WRQ

Minute virus of mice non-structural protein-1N-terminal nuclease domain reveals a unique Zn2+ coordination in the active site pocket and shows a novel mode of DNA recognition at the origin of replication

3WRQ の概要

• エントリーDOI: 10.2210/pdb3wrq/pdb
• 関連するPDBエントリー: 3WRN 3WRO 3WRR 3WRS 4PP4
• 分子名称: Non-capsid protein NS-1, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: nuclease activity, single and double stranded dna binding, nicking protein, replication
• 由来する生物種: Murine minute virus (MVM)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32402.09

構造登録者

Tewary, S.K.,Zhao, H.,Tang, L. (登録日: 2014-02-27, 公開日: 2015-01-21, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.53 Å)