2QVJ

Crystal structure of a vesicular stomatitis virus nucleocapsid protein Ser290Trp mutant

Summary for 2QVJ

• Entry DOI: 10.2210/pdb2qvj/pdb
• Descriptor: Nucleocapsid protein (1 entity in total)
• Functional Keywords: nucleocapsid, cytoplasm, ribonucleoprotein, rna-binding, viral nucleoprotein, virion, rna binding protein
• Biological source: Vesicular stomatitis Indiana virus
• Cellular location: Virion: P03521
• Total number of polymer chains: 5
• Total formula weight: 237159.42

Authors

Luo, M.,Green, T.J.,Zhang, X.,Tsao, J.,Qiu, S. (deposition date: 2007-08-08, release date: 2008-01-08, Last modification date: 2024-02-21)

Primary citation

Zhang, X.,Green, T.J.,Tsao, J.,Qiu, S.,Luo, M.
Role of intermolecular interactions of vesicular stomatitis virus nucleoprotein in RNA encapsidation.
J.Virol., 82:674-682, 2008

PubMed Abstract: The crystal structure of the vesicular stomatitis virus nucleoprotein (N) in complex with RNA reveals extensive and specific intermolecular interactions among the N molecules in the 10-member oligomer. What roles these interactions play in encapsidating RNA was studied by mutagenesis of the N protein. Three N mutants intended for disruption of the intermolecular interactions were designed and coexpressed with the phosphoprotein (P) in an Escherichia coli system previously described (T. J. Green et al., J. Virol. 74:9515-9524, 2000). Mutants N (Delta1-22), N (Delta347-352), and N (320-324, (Ala)(5)) lost RNA encapsidation and oligomerization but still bound with P. Another mutant, N (Ser290-->Trp), was able to form a stable ring-like N oligomer and bind with the P protein but was no longer able to encapsidate RNA. The crystal structure of N (Ser290-->Trp) at 2.8 A resolution showed that this mutant can maintain all the same intermolecular interactions as the wild-type N except for a slight unwinding of the N-terminal lobe. These results suggest that the intermolecular contacts among the N molecules are required for encapsidation of the viral RNA.

PubMed: 18003727
DOI: 10.1128/JVI.00935-07

Experimental method

X-RAY DIFFRACTION (2.8 Å)