2WZL
The Structure of the N-RNA Binding Domain of the Mokola virus Phosphoprotein
Summary for 2WZL
| Entry DOI | 10.2210/pdb2wzl/pdb |
| Descriptor | PHOSPHOPROTEIN, GLYCEROL (3 entities in total) |
| Functional Keywords | viral protein, rabies, virion, chaperone, nucleoprotein, rna replication |
| Biological source | MOKOLA VIRUS |
| Cellular location | Phosphoprotein: Virion. Isoform P2: Host cytoplasm (By similarity). Isoform P3: Host nucleus (By similarity): P0C569 |
| Total number of polymer chains | 1 |
| Total formula weight | 34343.12 |
| Authors | Assenberg, R.,Delmas, O.,Ren, J.,Vidalain, P.,Verma, A.,Larrous, F.,Graham, S.,Tangy, F.,Grimes, J.,Bourhy, H. (deposition date: 2009-11-30, release date: 2009-12-15, Last modification date: 2023-12-20) |
| Primary citation | Assenberg, R.,Delmas, O.,Ren, J.,Vidalain, P.,Verma, A.,Larrous, F.,Graham, S.,Tangy, F.,Grimes, J.,Bourhy, H. The Structure of the N-RNA Binding Domain of the Mokola Virus Phosphoprotein J.Virol., 84:1089-, 2010 Cited by PubMed Abstract: Mokola virus (MOKV) is a nonsegmented, negative-sense RNA virus that belongs to the Lyssavirus genus and Rhabdoviridae family. MOKV phosphoprotein P is an essential component of the replication and transcription complex and acts as a cofactor for the viral RNA-dependent RNA polymerase. P recruits the viral polymerase to the nucleoprotein-bound viral RNA (N-RNA) via an interaction between its C-terminal domain and the N-RNA complex. Here we present a structure for this domain of MOKV P, obtained by expression of full-length P in Escherichia coli, which was subsequently truncated during crystallization. The structure has a high degree of homology with P of rabies virus, another member of Lyssavirus genus, and to a lesser degree with P of vesicular stomatitis virus (VSV), a member of the related Vesiculovirus genus. In addition, analysis of the crystal packing of this domain reveals a potential binding site for the nucleoprotein N. Using both site-directed mutagenesis and yeast two-hybrid experiments to measure P-N interaction, we have determined the relative roles of key amino acids involved in this interaction to map the region of P that binds N. This analysis also reveals a structural relationship between the N-RNA binding domain of the P proteins of the Rhabdoviridae and the Paramyxoviridae. PubMed: 19906936DOI: 10.1128/JVI.01520-09 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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