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	Cryo-EM structures of Thogoto virus polymerase reveal unique RNA transcription and replication mechanisms among orthomyxoviruses.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 4620, Year 2024
Publish date	May 30, 2024
Authors	Lu Xue / Tiancai Chang / Zimu Li / Chenchen Wang / Heyu Zhao / Mei Li / Peng Tang / Xin Wen / Mengmeng Yu / Jiqin Wu / Xichen Bao / Xiaojun Wang / Peng Gong / Jun He / Xinwen Chen / Xiaoli Xiong /
PubMed Abstract	Influenza viruses and thogotoviruses account for most recognized orthomyxoviruses. Thogotoviruses, exemplified by Thogoto virus (THOV), are capable of infecting humans using ticks as vectors. THOV ...Influenza viruses and thogotoviruses account for most recognized orthomyxoviruses. Thogotoviruses, exemplified by Thogoto virus (THOV), are capable of infecting humans using ticks as vectors. THOV transcribes mRNA without the extraneous 5' end sequences derived from cap-snatching in influenza virus mRNA. Here, we report cryo-EM structures to characterize THOV polymerase RNA synthesis initiation and elongation. The structures demonstrate that THOV RNA transcription and replication are able to start with short dinucleotide primers and that the polymerase cap-snatching machinery is likely non-functional. Triggered by RNA synthesis, asymmetric THOV polymerase dimers can form without the involvement of host factors. We confirm that, distinctive from influenza viruses, THOV-polymerase RNA synthesis is weakly dependent of the host factors ANP32A/B/E in human cells. This study demonstrates varied mechanisms in RNA synthesis and host factor utilization among orthomyxoviruses, providing insights into the mechanisms behind thogotoviruses' broad-infectivity range.
External links	Nat Commun / PubMed:38816392 / PubMed Central
Methods	EM (single particle)
Resolution	2.3 - 3.16 Å
Structure data	39838 8z85 EMDB-39838, PDB-8z85: Cryo-EM structure of Thogoto virus polymerase in transcription pre-initiation conformation 1 Method: EM (single particle) / Resolution: 2.3 Å 39848 8z8j EMDB-39848, PDB-8z8j: Cryo-EM structure of Thogoto virus polymerase in transcription pre-initiation conformation 2 Method: EM (single particle) / Resolution: 3.16 Å 39849 8z8n EMDB-39849, PDB-8z8n: Cryo-EM structure of Thogoto virus polymerase in transcription pre-initiation conformation 3 Method: EM (single particle) / Resolution: 2.79 Å 39850 8z8x EMDB-39850, PDB-8z8x: Cryo-EM structure of Thogoto virus polymerase in a transcription initiation conformation Method: EM (single particle) / Resolution: 3.06 Å 39852 8z90 EMDB-39852, PDB-8z90: Cryo-EM structure of Thogoto virus polymerase in transcription initiation conformation 2 Method: EM (single particle) / Resolution: 2.87 Å 39855 8z97 EMDB-39855, PDB-8z97: Cryo-EM structure of Thogoto virus polymerase in transcription elongation conformation Method: EM (single particle) / Resolution: 2.65 Å 39856 8z98 EMDB-39856, PDB-8z98: Cryo-EM structure of Thogoto virus polymerase in transcription reception conformation Method: EM (single particle) / Resolution: 2.52 Å 39862 8z9h EMDB-39862, PDB-8z9h: Cryo-EM structure of Thogoto virus polymerase in a transcription elongation-reception conformation Method: EM (single particle) / Resolution: 2.7 Å 39867 8z9q EMDB-39867, PDB-8z9q: Cryo-EM structure of Thogoto virus polymerase in a replication reception conformation Method: EM (single particle) / Resolution: 2.33 Å 39868 8z9r EMDB-39868, PDB-8z9r: Cryo-EM structure of Thogoto virus polymerase in a replication elongation-reception conformation Method: EM (single particle) / Resolution: 2.58 Å
Chemicals	ChemComp-G2P: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogueYM ChemComp-V9G*: 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-(2'-O-METHYL)-ADENOSINE
Source	thogoto virus (isolate siar 126)
Keywords	TRANSCRIPTION / RNA virus Polymerase / RNA polymerase