6Z6B

Structure of full-length La Crosse virus L protein (polymerase)

This is a non-PDB format compatible entry.

Summary for 6Z6B

• Entry DOI: 10.2210/pdb6z6b/pdb
• Descriptor: RNA (5'-R(P*AP*GP*UP*AP*GP*UP*GP*UP*GP*C)-3'), RNA (5'-R(P*UP*UP*AP*GP*UP*AP*GP*UP*AP*CP*AP*CP*UP*AP*CP*U)-3'), RNA (5'-R(*GP*CP*UP*AP*CP*UP*AP*A)-3'), ... (5 entities in total)
• Functional Keywords: rna-dependent rna polymerase, viral protein
• Biological source: Bunyavirus La Crosse; More
• Total number of polymer chains: 8
• Total formula weight: 553770.84

Authors

Cusack, S.,Gerlach, P.,Reguera, J. (deposition date: 2020-05-28, release date: 2020-07-29, Last modification date: 2024-01-24)

Primary citation

Arragain, B.,Effantin, G.,Gerlach, P.,Reguera, J.,Schoehn, G.,Cusack, S.,Malet, H.
Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes.
Nat Commun, 11:3590-3590, 2020

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 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.

PubMed: 32681014
DOI: 10.1038/s41467-020-17349-4

Experimental method

X-RAY DIFFRACTION (3.961 Å)