Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insight into RNA synthesis by influenza D polymerase.
Journal, issue, pages	Nat Microbiol, Vol. 4, Issue 10, Page 1750-1759, Year 2019
Publish date	Jun 17, 2019
Authors	Qi Peng / Yuqian Liu / Ruchao Peng / Min Wang / Wei Yang / Hao Song / Yuhai Chen / Sheng Liu / Min Han / Xinzheng Zhang / Peiyi Wang / Jinghua Yan / Buchang Zhang / Jianxun Qi / Tao Deng / George F Gao / Yi Shi /
PubMed Abstract	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 ...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.
External links	Nat Microbiol / PubMed:31209309
Methods	EM (single particle)
Resolution	3.4 - 4.6 Å
Structure data	9577 6kv5 EMDB-9577: structure of influenza D virus apo polymerase PDB-6kv5: Structure of influenza D virus apo polymerase Method: EM (single particle) / Resolution: 4.6 Å 9578 6kuk EMDB-9578, PDB-6kuk: Structure of influenza D virus polymerase bound to vRNA promoter in mode A conformation (class A1) Method: EM (single particle) / Resolution: 3.9 Å 9579 6kup EMDB-9579, PDB-6kup: Structure of influenza D virus polymerase bound to vRNA promoter in Mode A conformation(Class A2) Method: EM (single particle) / Resolution: 4.3 Å 9580 6kut EMDB-9580: structure of influenza D virus polymerase bound to vRNA promoter in Mode B conformation (Class B2) PDB-6kut: Structure of influenza D virus polymerase bound to vRNA promoter in Mode B conformation (Class B2) Method: EM (single particle) / Resolution: 4.1 Å 9581 6kur EMDB-9581, PDB-6kur: Structure of influenza D virus polymerase bound to vRNA promoter in Mode B conformation (Class B1) Method: EM (single particle) / Resolution: 3.7 Å 9582 6kuu EMDB-9582, PDB-6kuu: Structure of influenza D virus polymerase bound to vRNA promoter in Mode B conformation (Class B3) Method: EM (single particle) / Resolution: 4.0 Å 9887 6kuj EMDB-9887, PDB-6kuj: Structure of influenza D virus polymerase bound to cRNA promoter in class 1 Method: EM (single particle) / Resolution: 3.44 Å 9888 6kuv EMDB-9888, PDB-6kuv: Structure of influenza D virus polymerase bound to cRNA promoter in class 2 Method: EM (single particle) / Resolution: 4.1 Å
Source	Thogotovirus influenza d virus (d/swine/oklahoma/1334/2011) Influenza D virus synthetic construct (others)
Keywords	VIRAL PROTEIN/RNA / influenza D virus / polymerase / cryo-EM / VIRAL PROTEIN-RNA complex / RNA BINDING PROTEIN / VIRAL PROTEIN