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 snapshots of La Crosse virus polymerase reveal the mechanisms underlying Peribunyaviridae replication and transcription.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 902, Year 2022
Publish date	Feb 16, 2022
Authors	Benoît Arragain / Quentin Durieux Trouilleton / Florence Baudin / Jan Provaznik / Nayara Azevedo / Stephen Cusack / Guy Schoehn / Hélène Malet /
PubMed Abstract	Segmented negative-strand RNA bunyaviruses encode a multi-functional polymerase that performs genome replication and transcription. Here, we establish conditions for in vitro activity of La Crosse ...Segmented negative-strand RNA bunyaviruses encode a multi-functional polymerase that performs genome replication and transcription. Here, we establish conditions for in vitro activity of La Crosse virus polymerase and visualize its conformational dynamics by cryo-electron microscopy, unveiling the precise molecular mechanics underlying its essential activities. We find that replication initiation is coupled to distal duplex promoter formation, endonuclease movement, prime-and-realign loop extension and closure of the polymerase core that direct the template towards the active site. Transcription initiation depends on C-terminal region closure and endonuclease movements that prompt primer cleavage prior to primer entry in the active site. Product realignment after priming, observed in replication and transcription, is triggered by the prime-and-realign loop. Switch to elongation results in polymerase reorganization and core region opening to facilitate template-product duplex formation in the active site cavity. The uncovered detailed mechanics should be helpful for the future design of antivirals counteracting bunyaviral life threatening pathogens.
External links	Nat Commun / PubMed:35173159 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 3.9 Å
Structure data	13038 7ori EMDB-13038, PDB-7ori: La Crosse virus polymerase at replication late-elongation stage Method: EM (single particle) / Resolution: 3.9 Å 13039 7orj EMDB-13039, PDB-7orj: La Crosse virus polymerase at transcription capped RNA cleavage stage Method: EM (single particle) / Resolution: 3.9 Å 13040 7ork EMDB-13040, PDB-7ork: La Crosse virus polymerase in transcription mode with cleaved capped RNA entering the polymerase active site Method: EM (single particle) / Resolution: 3.1 Å 13041 7orl EMDB-13041, PDB-7orl: La Crosse virus polymerase at transcription initiation stage Method: EM (single particle) / Resolution: 3.6 Å 13042 7orm EMDB-13042, PDB-7orm: La Crosse virus polymerase at transcription early-elongation stage Method: EM (single particle) / Resolution: 3.3 Å 13043 7orn EMDB-13043, PDB-7orn: La Crosse virus polymerase at replication initiation stage Method: EM (single particle) / Resolution: 2.8 Å 13044 7oro EMDB-13044, PDB-7oro: La Crosse virus polymerase at replication early-elongation stage Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-POP: PYROPHOSPHATE 2- ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-HOH: WATER ChemComp-GTG*: 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE
Source	la crosse orthobunyavirus bunyavirus la crosse la crosse virus homo sapiens (human)
Keywords	VIRAL PROTEIN / RNA-dependent RNA polymerase