5FMM

crystal structure of the mid, cap-binding, mid-link and 627 domains from avian influenza a virus polymerase PB2 subunit bound to M7GTP

Summary for 5FMM

• Entry DOI: 10.2210/pdb5fmm/pdb
• Related: 5FML 5FMQ 5FMZ
• Descriptor: INFLUENZA A PB2 SUBUNIT, 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE, CITRATE ANION, ... (4 entities in total)
• Functional Keywords: viral protein, influenza a pb2-c region containing mid, cap-binding, mid-link, 627 and nls domains
• Biological source: INFLUENZA A VIRUS
• Total number of polymer chains: 1
• Total formula weight: 55468.17

Authors

Thierry, E.,Pflug, A.,Hart, D.,Cusack, S. (deposition date: 2015-11-06, release date: 2016-01-13, Last modification date: 2024-01-10)

Primary citation

Thierry, E.,Guilligay, D.,Kosinski, J.,Bock, T.,Gaudon, S.,Round, A.,Pflug, A.,Hengrung, N.,El Omari, K.,Baudin, F.,Hart, D.J.,Beck, M.,Cusack, S.
Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of Pb2 Domains.
Mol.Cell, 61:125-, 2016

PubMed Abstract: Influenza virus polymerase transcribes or replicates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and initiates RNA synthesis by binding the conserved 3' and 5' vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase structure with a bound complementary cRNA 5' end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)-containing domain translocates ∼90 Å to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease assays show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the polymerase allows it to adopt alternative conformations that are likely important during polymerase maturation into active progeny RNPs.

PubMed: 26711008
DOI: 10.1016/J.MOLCEL.2015.11.016

Experimental method

X-RAY DIFFRACTION (2.4 Å)