Summary information and primary citation
- PDB-id
-
6z6g;
SNAP-derived features in text and
JSON formats
- Class
- replication
- Method
- cryo-EM (3.06 Å)
- Summary
- cryo-EM structure of la crosse virus polymerase at
pre-initiation stage
- Reference
-
Arragain B, Effantin G, Gerlach P, Reguera J, Schoehn G,
Cusack S, Malet H (2020): "Pre-initiation
and elongation structures of full-length La Crosse virus
polymerase reveal functionally important conformational
changes." Nat Commun, 11,
3590. doi: 10.1038/s41467-020-17349-4.
- Abstract
- Bunyavirales is an order of segmented negative-strand
RNA viruses comprising several life-threatening pathogens
against which no effective treatment is currently
available. Replication and transcription of the RNA genome
constitute essential processes performed by the virally
encoded multi-domain RNA-dependent RNA polymerase. Here, we
describe the complete high-resolution cryo-EM structure of
La Crosse virus polymerase. It reveals the presence of key
protruding C-terminal domains, notably the cap-binding
domain, which undergoes large movements related to its role
in transcription initiation, and a zinc-binding domain that
displays a fold not previously observed. We capture the
polymerase structure at pre-initiation and elongation
states, uncovering the coordinated movement of the priming
loop, mid-thumb ring linker and lid domain required
for the establishment of a ten-base-pair template-product
RNA duplex before strand separation into respective exit
tunnels. These structural details and the observed dynamics
of key functional elements will be instrumental for
structure-based development of polymerase inhibitors.
