6EB9
Crystal Structure of the Nipah Virus Phosphoprotein Multimerization Domain Delta 542-544
Summary for 6EB9
| Entry DOI | 10.2210/pdb6eb9/pdb |
| Descriptor | Phosphoprotein (2 entities in total) |
| Functional Keywords | phosphoprotein, rna-dependent rna polymerase, coiled coil, oligomerization, viral protein |
| Biological source | Nipah virus |
| Total number of polymer chains | 1 |
| Total formula weight | 12282.95 |
| Authors | Bruhn, J.F.,Saphire, E.O. (deposition date: 2018-08-06, release date: 2019-03-13, Last modification date: 2024-03-13) |
| Primary citation | Bruhn, J.F.,Hotard, A.L.,Spiropoulou, C.F.,Lo, M.K.,Saphire, E.O. A Conserved Basic Patch and Central Kink in the Nipah Virus Phosphoprotein Multimerization Domain Are Essential for Polymerase Function. Structure, 27:660-668.e4, 2019 Cited by PubMed Abstract: Nipah virus is a highly lethal zoonotic pathogen found in Southeast Asia that has caused human encephalitis outbreaks with 40%-70% mortality. NiV encodes its own RNA-dependent RNA polymerase within the large protein, L. Efficient polymerase activity requires the phosphoprotein, P, which tethers L to its template, the viral nucleocapsid. P is a multifunctional protein with modular domains. The central P multimerization domain is composed of a long, tetrameric coiled coil. We investigated the importance of structural features found in this domain for polymerase function using a newly constructed NiV bicistronic minigenome assay. We identified a conserved basic patch and central kink in the coiled coil that are important for polymerase function, with R555 being absolutely essential. This basic patch and central kink are conserved in the related human pathogens measles and mumps viruses, suggesting that this mechanism may be conserved. PubMed: 30799076DOI: 10.1016/j.str.2019.01.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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