8R3K
Influenza A/H7N9 polymerase in self-stalled pre-termination state, with Pol II pS5 CTD peptide mimic bound in site 1A/2A.
Summary for 8R3K
| Entry DOI | 10.2210/pdb8r3k/pdb |
| EMDB information | 18871 |
| Descriptor | Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2, ... (8 entities in total) |
| Functional Keywords | viral polymerase, viral protein |
| Biological source | Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9)) More |
| Total number of polymer chains | 6 |
| Total formula weight | 290654.38 |
| Authors | |
| Primary citation | Krischuns, T.,Arragain, B.,Isel, C.,Paisant, S.,Budt, M.,Wolff, T.,Cusack, S.,Naffakh, N. The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome. Nat Commun, 15:1064-1064, 2024 Cited by PubMed Abstract: The current model is that the influenza virus polymerase (FluPol) binds either to host RNA polymerase II (RNAP II) or to the acidic nuclear phosphoprotein 32 (ANP32), which drives its conformation and activity towards transcription or replication of the viral genome, respectively. Here, we provide evidence that the FluPol-RNAP II binding interface, beyond its well-acknowledged function in cap-snatching during transcription initiation, has also a pivotal role in replication of the viral genome. Using a combination of cell-based and in vitro approaches, we show that the RNAP II C-terminal-domain, jointly with ANP32, enhances FluPol replication activity. We observe successive conformational changes to switch from a transcriptase to a replicase conformation in the presence of the bound RNPAII C-terminal domain and propose a model in which the host RNAP II is the anchor for transcription and replication of the viral genome. Our data open new perspectives on the spatial coupling of viral transcription and replication and the coordinated balance between these two activities. PubMed: 38316757DOI: 10.1038/s41467-024-45205-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.43 Å) |
Structure validation
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