5DIL

Crystal structure of the effector domain of the NS1 protein from influenza virus B

Summary for 5DIL

• Entry DOI: 10.2210/pdb5dil/pdb
• Descriptor: Non-structural protein 1, IODIDE ION (3 entities in total)
• Functional Keywords: effector domain, rna binding, rna-binding protein, viral protein
• Biological source: Influenza B virus (B/Singapore/DSO_090134/2004)
• Total number of polymer chains: 2
• Total formula weight: 33671.40

Authors

Guan, R.,Hamilton, K.,Ma, L.,Montelione, G.T. (deposition date: 2015-09-01, release date: 2016-08-10, Last modification date: 2024-11-20)

Primary citation

Ma, L.C.,Guan, R.,Hamilton, K.,Aramini, J.M.,Mao, L.,Wang, S.,Krug, R.M.,Montelione, G.T.
A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus.
Structure, 24:1562-1572, 2016

PubMed Abstract: Influenza viruses cause a highly contagious respiratory disease in humans. The NS1 proteins of influenza A and B viruses (NS1A and NS1B proteins, respectively) are composed of two domains, a dimeric N-terminal domain and a C-terminal domain, connected by a flexible polypeptide linker. Here we report the 2.0-Å X-ray crystal structure and nuclear magnetic resonance studies of the NS1B C-terminal domain, which reveal a novel and unexpected basic RNA-binding site that is not present in the NS1A protein. We demonstrate that single-site alanine replacements of basic residues in this site lead to reduced RNA-binding activity, and that recombinant influenza B viruses expressing these mutant NS1B proteins are severely attenuated in replication. This novel RNA-binding site of NS1B is required for optimal influenza B virus replication. Most importantly, this study reveals an unexpected RNA-binding function in the C-terminal domain of NS1B, a novel function that distinguishes influenza B viruses from influenza A viruses.

PubMed: 27545620
DOI: 10.1016/j.str.2016.07.001

Experimental method

X-RAY DIFFRACTION (2.01 Å)