2FQM
Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
Summary for 2FQM
| Entry DOI | 10.2210/pdb2fqm/pdb |
| Descriptor | Phosphoprotein (2 entities in total) |
| Functional Keywords | negative strand rna virus, polymerase, replication, cofactor, viral protein |
| Biological source | Vesicular stomatitis Indiana virus |
| Cellular location | Virion: P04880 |
| Total number of polymer chains | 6 |
| Total formula weight | 50655.41 |
| Authors | Ding, H.,Green, T.J.,Lu, S.,Luo, M. (deposition date: 2006-01-18, release date: 2006-02-07, Last modification date: 2024-02-14) |
| Primary citation | Ding, H.,Green, T.J.,Lu, S.,Luo, M. Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus J.Virol., 80:2808-2814, 2006 Cited by PubMed Abstract: In the replication cycle of nonsegmented negative-strand RNA viruses, the viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein (N)-enwrapped RNA template during the RNA polymerase reaction. The viral phosphoprotein (P) is a polymerase cofactor essential for this recognition. We report here the 2.3-angstroms-resolution crystal structure of the central domain (residues 107 to 177) of P from vesicular stomatitis virus. The fold of this domain consists of a beta hairpin, an alpha helix, and another beta hairpin. The alpha helix provides the stabilizing force for forming a homodimer, while the two beta hairpins add additional stabilization by forming a four-stranded beta sheet through domain swapping between two molecules. This central dimer positions the N- and C-terminal domains of P to interact with the N and L proteins, allowing the L protein to specifically recognize the nucleocapsid-RNA template and to progress along the template while concomitantly assembling N with nascent RNA. The interdimer interactions observed in the noncrystallographic packing may offer insight into the mechanism of the RNA polymerase processive reaction along the viral nucleocapsid-RNA template. PubMed: 16501089DOI: 10.1128/JVI.80.6.2808-2814.2006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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