2JDQ

C-terminal domain of influenza A virus polymerase PB2 subunit in complex with human importin alpha5

Summary for 2JDQ

• Entry DOI: 10.2210/pdb2jdq/pdb
• Related: 2GMO
• Descriptor: IMPORTIN ALPHA-1 SUBUNIT, POLYMERASE BASIC PROTEIN 2 (3 entities in total)
• Functional Keywords: transport, pb2 subunit, nuclear protein, protein transport, armadillo repeats, influenza a virus rna-dependent rna polymerase, bipartite nuclear localisation signal, nuclear import adapter, human importin alpha5, host-virus interaction
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 4
• Total formula weight: 117345.85

Authors

Tarendeau, F.,Guilligay, D.,Mas, P.,Boulo, S.,Baudin, F.,Ruigrok, R.W.H.,Hart, D.J.,Cusack, S. (deposition date: 2007-01-11, release date: 2007-02-27, Last modification date: 2023-12-13)

Primary citation

Tarendeau, F.,Boudet, J.,Guilligay, D.,Mas, P.,Bougault, C.,Boulo, S.,Baudin, F.,Ruigrok, R.W.H.,Daigle, N.,Ellenberg, J.,Cusack, S.,Simorre, J.-P.,Hart, D.J.
Structure and Nuclear Import Function of the C- Terminal Domain of Influenza Virus Polymerase Pb2 Subunit
Nat.Struct.Mol.Biol., 14:229-, 2007

PubMed Abstract: The trimeric influenza virus polymerase, comprising subunits PA, PB1 and PB2, is responsible for transcription and replication of the segmented viral RNA genome. Using a novel library-based screening technique called expression of soluble proteins by random incremental truncation (ESPRIT), we identified an independently folded C-terminal domain from PB2 and determined its solution structure by NMR. Using green fluorescent protein fusions, we show that both the domain and the full-length PB2 subunit are efficiently imported into the nucleus dependent on a previously overlooked bipartite nuclear localization sequence (NLS). The crystal structure of the domain complexed with human importin alpha5 shows how the last 20 residues unfold to permit binding to the import factor. The domain contains three surface residues implicated in adaptation from avian to mammalian hosts. One of these tethers the NLS-containing peptide to the core of the domain in the unbound state.

PubMed: 17310249
DOI: 10.1038/NSMB1212

Experimental method

X-RAY DIFFRACTION (2.2 Å)