3j9b | pdb_00003j9b

Electron cryo-microscopy of an RNA polymerase

spinqualitylabelsall models 3j9b, resolution 4.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3j9b is a 10 chain structure with sequence from I96a0 and Influenza a virus (a/goose/guangdong/3/97(h5n1)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: UNK Gene: PA (Influenza A virus (A/Goose/Guangdong/3/97(H5N1))), PB1 (I96A0), PB2 (I96A0) Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RDRP_I96A0] RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs.[UniProtKB:P03431] Publication Abstract from PubMed 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 A, 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. Cryo-EM Structure of Influenza Virus RNA Polymerase Complex at 4.3 A Resolution.,Chang S, Sun D, Liang H, Wang J, Li J, Guo L, Wang X, Guan C, Boruah BM, Yuan L, Feng F, Yang M, Wang L, Wang Y, Wojdyla J, Li L, Wang J, Wang M, Cheng G, Wang HW, Liu Y Mol Cell. 2015 Jan 21. pii: S1097-2765(14)01009-0. doi:, 10.1016/j.molcel.2014.12.031. PMID:25620561 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNA polymerase

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