|Title||Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes.|
|Journal, issue, pages||Nat Commun, Vol. 11, Issue 1, Page 3590, Year 2020|
|Publish date||Jul 17, 2020|
|Authors||Benoît Arragain / Grégory Effantin / Piotr Gerlach / Juan Reguera / Guy Schoehn / Stephen Cusack / Hélène Malet /|
|PubMed 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 ...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.|
|External links||PubMed:32681014 / Publisher's page|
|Keywords||VIRAL PROTEIN / RNA-dependent RNA polymerase / REPLICATION / viral polymerase / transcription / polymerase / La Crosse virus|
|Methods||EM (single particle) / X-ray diffraction|
|Resolution||3.02 - 3.961 A|
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