Summary information and primary citation
- PDB-id
- 7las; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- replication, hydrolase-DNA
- Method
- cryo-EM (4.4 Å)
- Summary
- cryo-EM structure of pcv2 replicase bound to ssDNA
- Reference
- Tarasova E, Dhindwal S, Popp M, Hussain S, Khayat R (2021): "Mechanism of DNA Interaction and Translocation by the Replicase of a Circular Rep-Encoding Single-Stranded DNA Virus." Mbio, 12, e0076321. doi: 10.1128/mBio.00763-21.
- Abstract
- Circular Rep-encoding single-stranded DNA (CRESS-DNA) viruses infect members from all three domains of life (Archaea, Prokarya, and Eukarya). The replicase (Rep) from these viruses is responsible for initiating rolling circle replication (RCR) of their genomes. Rep is a multifunctional enzyme responsible for nicking and ligating ssDNA and unwinding double-stranded DNA (dsDNA). We report the structure of porcine circovirus 2 (PCV2) Rep bound to ADP and single-stranded DNA (ssDNA), and Rep bound to ADP and double-stranded DNA (dsDNA). The structures demonstrate Rep to be a member of the superfamily 3 (SF3) of ATPases Associated with diverse cellular Activities (AAA
