Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3OUO

Structure of the Nucleoprotein from Rift Valley Fever Virus

Summary for 3OUO
Entry DOI10.2210/pdb3ouo/pdb
Related3OV9
DescriptorNucleoprotein, NITRITE ION (3 entities in total)
Functional Keywordsorthogonal bundle, viral genomic rna encapsidation, rna viral nucleoprotein, viral protein
Biological sourceRift valley fever virus (RVFV)
Cellular locationVirion: P21700
Total number of polymer chains3
Total formula weight84229.19
Authors
Ferron, F.,Danek, E.I.,Li, Z.,Luo, D.,Wong, Y.H.,Coutard, B.,Lantez, V.,Charrel, R.,Canard, B.,Walz, T.,Lescar, J. (deposition date: 2010-09-15, release date: 2011-05-25, Last modification date: 2024-11-20)
Primary citationFerron, F.,Li, Z.,Danek, E.I.,Luo, D.,Wong, Y.,Coutard, B.,Lantez, V.,Charrel, R.,Canard, B.,Walz, T.,Lescar, J.
The hexamer structure of Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
Plos Pathog., 7:e1002030-e1002030, 2011
Cited by
PubMed Abstract: Rift Valley fever virus (RVFV), a Phlebovirus with a genome consisting of three single-stranded RNA segments, is spread by infected mosquitoes and causes large viral outbreaks in Africa. RVFV encodes a nucleoprotein (N) that encapsidates the viral RNA. The N protein is the major component of the ribonucleoprotein complex and is also required for genomic RNA replication and transcription by the viral polymerase. Here we present the 1.6 Å crystal structure of the RVFV N protein in hexameric form. The ring-shaped hexamers form a functional RNA binding site, as assessed by mutagenesis experiments. Electron microscopy (EM) demonstrates that N in complex with RNA also forms rings in solution, and a single-particle EM reconstruction of a hexameric N-RNA complex is consistent with the crystallographic N hexamers. The ring-like organization of the hexamers in the crystal is stabilized by circular interactions of the N terminus of RVFV N, which forms an extended arm that binds to a hydrophobic pocket in the core domain of an adjacent subunit. The conformation of the N-terminal arm differs from that seen in a previous crystal structure of RVFV, in which it was bound to the hydrophobic pocket in its own core domain. The switch from an intra- to an inter-molecular interaction mode of the N-terminal arm may be a general principle that underlies multimerization and RNA encapsidation by N proteins from Bunyaviridae. Furthermore, slight structural adjustments of the N-terminal arm would allow RVFV N to form smaller or larger ring-shaped oligomers and potentially even a multimer with a super-helical subunit arrangement. Thus, the interaction mode between subunits seen in the crystal structure would allow the formation of filamentous ribonucleocapsids in vivo. Both the RNA binding cleft and the multimerization site of the N protein are promising targets for the development of antiviral drugs.
PubMed: 21589902
DOI: 10.1371/journal.ppat.1002030
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon