2ZNL

Crystal structure of PA-PB1 complex form influenza virus RNA polymerase

Summary for 2ZNL

• Entry DOI: 10.2210/pdb2znl/pdb
• Descriptor: Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit (3 entities in total)
• Functional Keywords: influenza a virus, rna polymerase, pa, pb1, subunit interaction, phosphoprotein, nucleotide-binding, nucleotidyltransferase, rna replication, rna-directed rna polymerase, transferase, transcription
• Biological source: Influenza A virus; More
• Cellular location: Host nucleus (Potential): P03431
• Total number of polymer chains: 2
• Total formula weight: 63530.15

Authors

Obayashi, E.,Yoshida, H.,Kawai, F.,Shibayama, N.,Kawaguchi, A.,Nagata, K.,Tame, J.R.H.,Park, S.-Y. (deposition date: 2008-04-28, release date: 2008-09-02, Last modification date: 2024-03-13)

Primary citation

Obayashi, E.,Yoshida, H.,Kawai, F.,Shibayama, N.,Kawaguchi, A.,Nagata, K.,Tame, J.R.H.,Park, S.-Y.
The structural basis for an essential subunit interaction in influenza virus RNA polymerase
Nature, 454:1127-1131, 2008

PubMed Abstract: Influenza A virus is a major human and animal pathogen with the potential to cause catastrophic loss of life. The virus reproduces rapidly, mutates frequently and occasionally crosses species barriers. The recent emergence in Asia of avian influenza related to highly pathogenic forms of the human virus has highlighted the urgent need for new effective treatments. Here we demonstrate the importance to viral replication of a subunit interface in the viral RNA polymerase, thereby providing a new set of potential drug binding sites entirely independent of surface antigen type. No current medication targets this heterotrimeric polymerase complex. All three subunits, PB1, PB2 and PA, are required for both transcription and replication. PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA is involved in assembly of the functional complex, but so far very little structural information has been reported for any of them. We describe the crystal structure of a large fragment of one subunit (PA) of influenza A RNA polymerase bound to a fragment of another subunit (PB1). The carboxy-terminal domain of PA forms a novel fold, and forms a deep, highly hydrophobic groove into which the amino-terminal residues of PB1 can fit by forming a 3(10) helix.

PubMed: 18660801
DOI: 10.1038/nature07225

Experimental method

X-RAY DIFFRACTION (2.3 Å)