3PMK

Crystal structure of the Vesicular Stomatitis Virus RNA free nucleoprotein/phosphoprotein complex

Summary for 3PMK

• Entry DOI: 10.2210/pdb3pmk/pdb
• Related: 2GIC
• Descriptor: Nucleocapsid protein, Phosphoprotein (3 entities in total)
• Functional Keywords: chaperone, viral protein
• Biological source: Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP; More
• Total number of polymer chains: 10
• Total formula weight: 267485.78

Authors

Leyrat, C.,Yabukarski, F.,Tarbouriech, N.,Ruigrok, R.W.H.,Jamin, M. (deposition date: 2010-11-17, release date: 2011-10-05, Last modification date: 2023-09-06)

Primary citation

Leyrat, C.,Yabukarski, F.,Tarbouriech, N.,Ribeiro, E.A.,Jensen, M.R.,Blackledge, M.,Ruigrok, R.W.,Jamin, M.
Structure of the Vesicular Stomatitis Virus N0-P Complex
Plos Pathog., 7:e1002248-e1002248, 2011

PubMed Abstract: Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (N(Δ21)) and a peptide of 60 amino acids (P(60)) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N(0)). The complex crystallized in a decameric circular form, which was solved at 3.0 Å resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization. Small-angle X-ray scattering experiment and NMR spectroscopy on the soluble complex confirms the binding of the MoRE and indicates that its flanking regions remain flexible in the complex. The structure of this complex also suggests a mechanism for the initiation of viral RNA synthesis.

PubMed: 21960769
DOI: 10.1371/journal.ppat.1002248

Experimental method

X-RAY DIFFRACTION (3.03 Å)