Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes.

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 l

SUBMITTER: Arragain B 

PROVIDER: S-EPMC7368059 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature