3OUO

Structure of the Nucleoprotein from Rift Valley Fever Virus

Summary for 3OUO

• Entry DOI: 10.2210/pdb3ouo/pdb
• Related: 3OV9
• Descriptor: Nucleoprotein, NITRITE ION (3 entities in total)
• Functional Keywords: orthogonal bundle, viral genomic rna encapsidation, rna viral nucleoprotein, viral protein
• Biological source: Rift valley fever virus (RVFV)
• Cellular location: Virion: P21700
• Total number of polymer chains: 3
• Total formula weight: 84229.19

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 citation

Ferron, 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

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)