2yi8
Structure of the RNA polymerase VP1 from Infectious Pancreatic Necrosis VirusStructure of the RNA polymerase VP1 from Infectious Pancreatic Necrosis Virus
Structural highlights
FunctionRDRP_IPNVJ RNA-dependent RNA polymerase which is found both free and covalently attached to the genomic RNA. May also contain guanylyl and methyl transferase activities (By similarity). Publication Abstract from PubMedThe RNA-dependent RNA polymerase VP1 of infectious pancreatic necrosis virus (IPNV) is a single polypeptide responsible for both viral RNA transcription and genome replication. Sequence analysis identifies IPNV VP1 as having an unusual active site topology. We have purified, crystallized and solved the structure of IPNV VP1 to 2.3 A resolution in its apo form and at 2.2 A resolution bound to the catalytically-activating metal magnesium. We find that recombinantly-expressed VP1 is highly active for RNA transcription and replication, yielding both free and polymerase-attached RNA products. IPNV VP1 also possesses terminal (deoxy)nucleotide transferase, RNA-dependent DNA polymerase (reverse transcriptase) and template-independent self-guanylylation activity. The N-terminus of VP1 interacts with the active-site cleft and we show that the N-terminal serine residue is required for formation of covalent RNAratiopolymerase complexes, providing a mechanism for the genesis of viral genomeratiopolymerase complexes observed in vivo. The N-terminus of the RNA polymerase from infectious pancreatic necrosis virus is the determinant of genome attachment.,Graham SC, Sarin LP, Bahar MW, Myers RA, Stuart DI, Bamford DH, Grimes JM PLoS Pathog. 2011 Jun;7(6):e1002085. Epub 2011 Jun 23. PMID:21731487[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||