3J9B

Electron cryo-microscopy of an RNA polymerase

Summary for 3J9B

• Entry DOI: 10.2210/pdb3j9b/pdb
• EMDB information: 6202
• Descriptor: Polymerase, RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2, ... (6 entities in total)
• Functional Keywords: influenza rdrp, single particle reconstitution, replication, rna binding protein-transferase-rna complex, rna binding protein/transferase/rna
• Biological source: Influenza A virus; More
• Total number of polymer chains: 10
• Total formula weight: 208770.36

Authors

Chang, S.H.,Sun, D.P.,Liang, H.H.,Wang, J.,Li, J.,Guo, L.,Wang, X.L.,Guan, C.C.,Boruah, B.M.,Yuan, L.M.,Feng, F.,Yang, M.R.,Wojdyla, J.,Wang, J.W.,Wang, M.T.,Wang, H.W.,Liu, Y.F. (deposition date: 2014-12-16, release date: 2015-02-18, Last modification date: 2024-03-20)

Primary citation

Chang, S.,Sun, D.,Liang, H.,Wang, J.,Li, J.,Guo, L.,Wang, X.,Guan, C.,Boruah, B.M.,Yuan, L.,Feng, F.,Yang, M.,Wang, L.,Wang, Y.,Wojdyla, J.,Li, L.,Wang, J.,Wang, M.,Cheng, G.,Wang, H.W.,Liu, Y.
Cryo-EM Structure of Influenza Virus RNA Polymerase Complex at 4.3 angstrom Resolution.
Mol.Cell, 2015

PubMed Abstract: Replication and transcription of influenza virus genome mainly depend on its RNA-dependent RNA polymerase (RdRP), composed of the PA, PB1, and PB2 subunits. Although extensively studied, the underlying mechanism of the RdRP complex is still unclear. Here we report the biochemical characterization of influenza RdRP subcomplex comprising PA, PB1, and N terminus of PB2, which exist as dimer in solution and can assemble into a tetramer state, regulated by vRNA promoter. Using single-particle cryo-electron microscopy, we have reconstructed the RdRP tetramer complex at 4.3 Å, highlighting the assembly and interfaces between monomers within the tetrameric structure. The individual RdRP subcomplex contains all the characterized motifs and appears as a cage-like structure. High-throughput mutagenesis profiling revealed that residues involved in the oligomer state formation are critical for viral life cycle. Our results lay a solid base for understanding the mechanism of replication of influenza and other negative-stranded RNA viruses.

PubMed: 25620561
DOI: 10.1016/j.molcel.2014.12.031

Experimental method

ELECTRON MICROSCOPY (4.3 Å)