3LYF

Crystal Structure of the Rift Valley Fever Virus Nucleocapsid Protein

Summary for 3LYF

• Entry DOI: 10.2210/pdb3lyf/pdb
• Descriptor: Nucleocapsid protein, GLYCEROL (3 entities in total)
• Functional Keywords: nucleocapsid protein, n protein, rift valley fever virus, ribonucleoprotein, viral nucleoprotein, viral protein
• Biological source: Rift Valley fever virus (RVFV)
• Total number of polymer chains: 4
• Total formula weight: 109834.56

Authors

Raymond, D.D.,Smith, J.L. (deposition date: 2010-02-26, release date: 2010-06-30, Last modification date: 2024-02-21)

Primary citation

Raymond, D.D.,Piper, M.E.,Gerrard, S.R.,Smith, J.L.
Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation.
Proc.Natl.Acad.Sci.USA, 107:11769-11774, 2010

PubMed Abstract: Rift Valley fever virus (RVFV) is a negative-sense RNA virus (genus Phlebovirus, family Bunyaviridae) that infects livestock and humans and is endemic to sub-Saharan Africa. Like all negative-sense viruses, the segmented RNA genome of RVFV is encapsidated by a nucleocapsid protein (N). The 1.93-A crystal structure of RVFV N and electron micrographs of ribonucleoprotein (RNP) reveal an encapsidated genome of substantially different organization than in other negative-sense RNA virus families. The RNP polymer, viewed in electron micrographs of both virus RNP and RNP reconstituted from purified N with a defined RNA, has an extended structure without helical symmetry. N-RNA species of approximately 100-kDa apparent molecular weight and heterogeneous composition were obtained by exhaustive ribonuclease treatment of virus RNP, by recombinant expression of N, and by reconstitution from purified N and an RNA oligomer. RNA-free N, obtained by denaturation and refolding, has a novel all-helical fold that is compact and well ordered at both the N and C termini. Unlike N of other negative-sense RNA viruses, RVFV N has no positively charged surface cleft for RNA binding and no protruding termini or loops to stabilize a defined N-RNA oligomer or RNP helix. A potential protein interaction site was identified in a conserved hydrophobic pocket. The nonhelical appearance of phlebovirus RNP, the heterogeneous approximately 100-kDa N-RNA multimer, and the N fold differ substantially from the RNP and N of other negative-sense RNA virus families and provide valuable insights into the structure of the encapsidated phlebovirus genome.

PubMed: 20547879
DOI: 10.1073/pnas.1001760107

Experimental method

X-RAY DIFFRACTION (1.93 Å)