6t0w | pdb_00006t0w

Human Influenza B polymerase recycling complex

spinqualitylabelsall models 6t0w, resolution 3.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6t0w is a 4 chain structure with sequence from 9infb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: PA (9INFB), PB1 (9INFB), PB2 (9INFB) Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A4Y5WMY1_9INFB] Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds a wide range of cap structures of target pre-RNAs which are subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex.[HAMAP-Rule:MF_04062] 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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