8QE5

Apo Hantaan virus polymerase in monomeric state

Summary for 8QE5

• Entry DOI: 10.2210/pdb8qe5/pdb
• EMDB information: 18343
• Descriptor: RNA-directed RNA polymerase L (1 entity in total)
• Functional Keywords: bunyavirus, hantaan virus, polymerase, dimer, viral protein
• Biological source: Hantaan virus 76-118
• Total number of polymer chains: 1
• Total formula weight: 249476.48

Authors

Durieux Trouilleton, Q.,Arragain, B.,Malet, H. (deposition date: 2023-08-30, release date: 2024-03-27)

Primary citation

Durieux Trouilleton, Q.,Housset, D.,Tarillon, P.,Arragain, B.,Malet, H.
Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers.
Nat Commun, 15:2256-2256, 2024

PubMed Abstract: Hantaan virus is a dangerous human pathogen whose segmented negative-stranded RNA genome is replicated and transcribed by a virally-encoded multi-functional polymerase. Here we describe the complete cryo-electron microscopy structure of Hantaan virus polymerase in several oligomeric forms. Apo polymerase protomers can adopt two drastically different conformations, which assemble into two distinct symmetric homodimers, that can themselves gather to form hexamers. Polymerase dimerization induces the stabilization of most polymerase domains, including the C-terminal domain that contributes the most to dimer's interface, along with a lariat region that participates to the polymerase steadying. Binding to viral RNA induces significant conformational changes resulting in symmetric oligomer disruption and polymerase activation, suggesting the possible involvement of apo multimers as protecting systems that would stabilize the otherwise flexible C-terminal domains. Overall, these results provide insights into the multimerization capability of Hantavirus polymerase and may help to define antiviral compounds to counteract these life-threatening viruses.

PubMed: 38480734
DOI: 10.1038/s41467-024-46601-4

Experimental method

ELECTRON MICROSCOPY (2.6 Å)