6VAG
Crystal structure of the oligomerization domain of phosphoprotein from parainfluenza virus 5
Summary for 6VAG
| Entry DOI | 10.2210/pdb6vag/pdb |
| Descriptor | Phosphoprotein, GLYCEROL (3 entities in total) |
| Functional Keywords | paramyxovirus, phosphoprotein, oligomerization domain, viral protein |
| Biological source | Parainfluenza virus 5 (strain W3) (PIV5) |
| Total number of polymer chains | 2 |
| Total formula weight | 23538.86 |
| Authors | Aggarwal, M.,Abdella, R.,He, Y.,Lamb, R.A. (deposition date: 2019-12-17, release date: 2020-02-19, Last modification date: 2024-04-03) |
| Primary citation | Abdella, R.,Aggarwal, M.,Okura, T.,Lamb, R.A.,He, Y. Structure of a paramyxovirus polymerase complex reveals a unique methyltransferase-CTD conformation. Proc.Natl.Acad.Sci.USA, 117:4931-4941, 2020 Cited by PubMed Abstract: Paramyxoviruses are enveloped, nonsegmented, negative-strand RNA viruses that cause a wide spectrum of human and animal diseases. The viral genome, packaged by the nucleoprotein (N), serves as a template for the polymerase complex, composed of the large protein (L) and the homo-tetrameric phosphoprotein (P). The ∼250-kDa L possesses all enzymatic activities necessary for its function but requires P in vivo. Structural information is available for individual P domains from different paramyxoviruses, but how P interacts with L and how that affects the activity of L is largely unknown due to the lack of high-resolution structures of this complex in this viral family. In this study we determined the structure of the L-P complex from parainfluenza virus 5 (PIV5) at 4.3-Å resolution using cryoelectron microscopy, as well as the oligomerization domain (OD) of P at 1.4-Å resolution using X-ray crystallography. P-OD associates with the RNA-dependent RNA polymerase domain of L and protrudes away from it, while the X domain of one chain of P is bound near the L nucleotide entry site. The methyltransferase (MTase) domain and the C-terminal domain (CTD) of L adopt a unique conformation, positioning the MTase active site immediately above the poly-ribonucleotidyltransferase domain and near the likely exit site for the product RNA 5' end. Our study reveals a potential mechanism that mononegavirus polymerases may employ to switch between transcription and genome replication. This knowledge will assist in the design and development of antivirals against paramyxoviruses. PubMed: 32075920DOI: 10.1073/pnas.1919837117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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