7PKP

NSP2 RNP complex

Summary for 7PKP

• Entry DOI: 10.2210/pdb7pkp/pdb
• EMDB information: 13476
• Descriptor: Non-structural protein 2 (1 entity in total)
• Functional Keywords: rna chaperone rna folding rotavirus, viral protein
• Biological source: Rotavirus A
• Total number of polymer chains: 8
• Total formula weight: 289878.56

Authors

Bravo, J.P.K.,Borodavka, A. (deposition date: 2021-08-26, release date: 2021-09-29, Last modification date: 2025-07-02)

Primary citation

Bravo, J.P.K.,Bartnik, K.,Venditti, L.,Acker, J.,Gail, E.H.,Colyer, A.,Davidovich, C.,Lamb, D.C.,Tuma, R.,Calabrese, A.N.,Borodavka, A.
Structural basis of rotavirus RNA chaperone displacement and RNA annealing.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Rotavirus genomes are distributed between 11 distinct RNA molecules, all of which must be selectively copackaged during virus assembly. This likely occurs through sequence-specific RNA interactions facilitated by the RNA chaperone NSP2. Here, we report that NSP2 autoregulates its chaperone activity through its C-terminal region (CTR) that promotes RNA-RNA interactions by limiting its helix-unwinding activity. Unexpectedly, structural proteomics data revealed that the CTR does not directly interact with RNA, while accelerating RNA release from NSP2. Cryo-electron microscopy reconstructions of an NSP2-RNA complex reveal a highly conserved acidic patch on the CTR, which is poised toward the bound RNA. Virus replication was abrogated by charge-disrupting mutations within the acidic patch but completely restored by charge-preserving mutations. Mechanistic similarities between NSP2 and the unrelated bacterial RNA chaperone Hfq suggest that accelerating RNA dissociation while promoting intermolecular RNA interactions may be a widespread strategy of RNA chaperone recycling.

PubMed: 34615715
DOI: 10.1073/pnas.2100198118

Experimental method

ELECTRON MICROSCOPY (3.1 Å)