6tw1 | pdb_00006tw1

Bat Influenza A polymerase termination complex with pyrophosphate using 44-mer vRNA template with mutated oligo(U) sequence

spinqualitylabelsall models 6tw1, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tw1 is a 5 chain structure with sequence from Influenza a virus (a/little yellow-shouldered bat/guatemala/060/2010(h17n10)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: M4H, MG, POP Gene: PA (Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10))), PB1 (Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10))), PB2 (Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10))) Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Influenza polymerase uses unique mechanisms to synthesize capped and polyadenylated mRNAs from the genomic viral RNA (vRNA) template, which is packaged inside ribonucleoprotein particles (vRNPs). Here, we visualize by cryoelectron microscopy the conformational dynamics of the polymerase during the complete transcription cycle from pre-initiation to termination, focusing on the template trajectory. After exiting the active site cavity, the template 3' extremity rebinds into a specific site on the polymerase surface. Here, it remains sequestered during all subsequent transcription steps, forcing the template to loop out as it further translocates. At termination, the strained connection between the bound template 5' end and the active site results in polyadenylation by stuttering at uridine 17. Upon product dissociation, further conformational changes release the trapped template, allowing recycling back into the pre-initiation state. Influenza polymerase thus performs transcription while tightly binding to and protecting both template ends, allowing efficient production of multiple mRNAs from a single vRNP. A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase.,Wandzik JM, Kouba T, Karuppasamy M, Pflug A, Drncova P, Provaznik J, Azevedo N, Cusack S Cell. 2020 Apr 16. pii: S0092-8674(20)30389-5. doi: 10.1016/j.cell.2020.03.061. PMID:32304664 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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