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TitlePre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 3590, Year 2020
Publish dateJul 17, 2020
AuthorsBenoît Arragain / Grégory Effantin / Piotr Gerlach / Juan Reguera / Guy Schoehn / Stephen Cusack / Hélène Malet /
PubMed AbstractBunyavirales 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 linksNat Commun / PubMed:32681014 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.02 - 3.961 Å
Structure data

11093

6z6g

EMDB-11093: Cryo-EM map of La Crosse virus polymerase at pre-initiation stage
PDB-6z6g: Cryo-EM structure of La Crosse virus polymerase at pre-initiation stage
Method: EM (single particle) / Resolution: 3.06 Å

EMDB-11095:
Masked cryo-EM map of La Crosse virus polymerase cap-binding domain and mid domain
Method: EM (single particle) / Resolution: 3.54 Å

EMDB-11107:
Masked cryo-EM map of La Crosse virus polymerase zinc-binding domain and mid domain
Method: EM (single particle) / Resolution: 3.49 Å

11118

6z8k

EMDB-11118, PDB-6z8k:
La Crosse virus polymerase at elongation mimicking stage
Method: EM (single particle) / Resolution: 3.02 Å

PDB-6z6b:
Structure of full-length La Crosse virus L protein (polymerase)
Method: X-RAY DIFFRACTION / Resolution: 3.961 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • bunyavirus la crosse
  • la crosse orthobunyavirus
KeywordsVIRAL PROTEIN / RNA-dependent RNA polymerase / REPLICATION / viral polymerase / transcription / polymerase / La Crosse virus

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