8XMS

Crystal structure of Porcine Circovirus type II Rep ATPase domain

8XMS の概要

• エントリーDOI: 10.2210/pdb8xms/pdb
• 分子名称: Replication-associated protein (2 entities in total)
• 機能のキーワード: replication, atpase, viral protein., viral protein
• 由来する生物種: Porcine circovirus 2
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 113112.54

構造登録者

Guan, S.Y.,Song, Y.F. (登録日: 2023-12-28, 公開日: 2024-04-17)

主引用文献

Guan, S.,Li, Z.,Han, Y.,Tian, A.,Zhou, S.,Chen, H.,Peng, G.,Song, Y.
Crystal structure of the ATPase domain of porcine circovirus type 2 Rep protein.
J.Gen.Virol., 105:-, 2024

PubMed Abstract: PCV2 belongs to the genus in the family , whose genome is replicated by rolling circle replication (RCR). PCV2 Rep is a multifunctional enzyme that performs essential functions at multiple stages of viral replication. Rep is responsible for nicking and ligating single-stranded DNA and unwinding double-stranded DNA (dsDNA). However, the structure and function of the Rep are still poorly understood, which significantly impedes viral replication research. This study successfully resolved the structure of the PCV2 Rep ATPase domain (PRAD) using X-ray crystallography. Homologous structure search revealed that Rep belonged to the superfamily 3 (SF3) helicase, and multiple conserved residues were identified during sequence alignment with SF3 family members. Simultaneously, a hexameric PRAD model was generated for analysing characteristic structures and sites. Mutation of the conserved site and measurement of its activity showed that the hallmark motifs of the SF3 family influenced helicase activity by affecting ATPase activity and β-hairpin just caused the loss of helicase activity. The structural and functional analyses of the PRAD provide valuable insights for future research on PCV2 replication and antiviral strategies.

PubMed: 38506716
DOI: 10.1099/jgv.0.001972

実験手法

X-RAY DIFFRACTION (2.2 Å)