6kuv

Structure of influenza D virus polymerase bound to cRNA promoter in class 2

spinqualitylabelsall models 6kuv, resolution 4.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kuv is a 5 chain structure. This structure supersedes the now removed PDB entry 6ju3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The influenza virus polymerase uses capped RNA primers to initiate transcription, and a combination of terminal and internal de novo initiations for the two-step replication process by binding the conserved viral genomic RNA (vRNA) or complementary RNA (cRNA) promoter. Here, we determined the apo and promoter-bound influenza D polymerase structures using cryo-electron microscopy and found the polymerase has an evolutionarily conserved stable core structure with inherently flexible peripheral domains. Strikingly, two conformations (mode A and B) of the vRNA promoter were observed where the 3'-vRNA end can bind at two different sites, whereas the cRNA promoter only binds in the mode B conformation. Functional studies confirmed the critical role of the mode B conformation for vRNA synthesis via the intermediate cRNA but not for cRNA production, which is mainly regulated by the mode A conformation. Both conformations participate in the regulation of the transcription process. This work advances our understanding of the regulatory mechanisms for the synthesis of different RNA species by influenza virus polymerase and opens new opportunities for antiviral drug design. Structural insight into RNA synthesis by influenza D polymerase.,Peng Q, Liu Y, Peng R, Wang M, Yang W, Song H, Chen Y, Liu S, Han M, Zhang X, Wang P, Yan J, Zhang B, Qi J, Deng T, Gao GF, Shi Y Nat Microbiol. 2019 Jun 17. pii: 10.1038/s41564-019-0487-5. doi:, 10.1038/s41564-019-0487-5. PMID:31209309 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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