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Volume 105, Issue 3

Crystal structure of the ATPase domain of porcine circovirus type 2 Rep protein No Access

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.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): ATPase activity , crystal structure , helicase activity , porcine circovirus type 2 (PCV2) and Rep ATPase domain
Funding
This study was supported by the:
  • National Natural Science Foundation of China (Award 31972658)
    • Principle Award Recipient: YunfengSong
© 2024 The Authors
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2024-03-20
2024-04-27
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Crystal structure of the ATPase domain of porcine circovirus type 2 Rep protein
J. Gen. Virol. 105, 001972 (2024); https://doi.org/10.1099/jgv.0.001972
/content/journal/jgv/10.1099/jgv.0.001972
/content/journal/jgv/10.1099/jgv.0.001972
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