2YI8
Structure of the RNA polymerase VP1 from Infectious Pancreatic Necrosis Virus
Summary for 2YI8
Entry DOI | 10.2210/pdb2yi8/pdb |
Related | 2YI9 2YIA 2YIB |
Descriptor | RNA-DIRECTED RNA POLYMERASE, POTASSIUM ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | transferase, reverse transcriptase, ipnv |
Biological source | INFECTIOUS PANCREATIC NECROSIS VIRUS |
Total number of polymer chains | 5 |
Total formula weight | 448291.33 |
Authors | Graham, S.C.,Sarin, L.P.,Bahar, M.W.,Myers, R.A.,Stuart, D.I.,Bamford, D.H.,Grimes, J.M. (deposition date: 2011-05-11, release date: 2011-07-20, Last modification date: 2023-12-20) |
Primary citation | Graham, S.C.,Sarin, L.P.,Bahar, M.W.,Myers, R.A.,Stuart, D.I.,Bamford, D.H.,Grimes, J.M. The N-Terminus of the RNA Polymerase from Infectious Pancreatic Necrosis Virus is the Determinant of Genome Attachment. Plos Pathog., 7:2085-, 2011 Cited by PubMed Abstract: The 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 Å resolution in its apo form and at 2.2 Å 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 RNA:polymerase complexes, providing a mechanism for the genesis of viral genome:polymerase complexes observed in vivo. PubMed: 21731487DOI: 10.1371/JOURNAL.PPAT.1002085 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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