3A1G
High-Resolution Crystal Structure of RNA polymerase PB1-PB2 subunits from Influenza A Virus
Summary for 3A1G
| Entry DOI | 10.2210/pdb3a1g/pdb |
| Related | 2ZTT |
| Descriptor | RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2 (3 entities in total) |
| Functional Keywords | influenza virus, rna polymerase, nucleotide-binding, nucleotidyltransferase, nucleus, rna replication, rna-directed rna polymerase, transferase, mitochondrion, mrna capping, mrna processing, virion |
| Biological source | Influenza A virus (A/Puerto Rico/8/34(H1N1)) More |
| Cellular location | Host nucleus (Potential): P03431 Virion: P03428 |
| Total number of polymer chains | 4 |
| Total formula weight | 28813.13 |
| Authors | Sugiyama, K.,Park, S.-Y.,Obayashi, E. (deposition date: 2009-04-02, release date: 2009-06-09, Last modification date: 2024-10-23) |
| Primary citation | Sugiyama, K.,Obayashi, E.,Kawaguchi, A.,Suzuki, Y.,Tame, J.R.H.,Nagata, K.,Park, S.-Y. Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase Embo J., 28:1803-1811, 2009 Cited by PubMed Abstract: Influenza virus RNA-dependent RNA polymerase is a multi-functional heterotrimer, which uses a 'cap-snatching' mechanism to produce viral mRNA. Host cell mRNA is cleaved to yield a cap-bearing oligonucleotide, which can be extended using viral genomic RNA as a template. The cap-binding and endonuclease activities are only activated once viral genomic RNA is bound. This requires signalling from the RNA-binding PB1 subunit to the cap-binding PB2 subunit, and the interface between these two subunits is essential for the polymerase activity. We have defined this interaction surface by protein crystallography and tested the effects of mutating contact residues on the function of the holo-enzyme. This novel interface is surprisingly small, yet, it has a crucial function in regulating the 250 kDa polymerase complex and is completely conserved among avian and human influenza viruses. PubMed: 19461581DOI: 10.1038/emboj.2009.138 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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