3PTO

Crystal Structure of an empty Vesicular Stomatitis Virus Nucleocapsid Protein Complex

Summary for 3PTO

• Entry DOI: 10.2210/pdb3pto/pdb
• Related: 3PTX 3PU0 3PU1 3PU4
• Descriptor: Nucleoprotein, URANYL (VI) ION (2 entities in total)
• Functional Keywords: nucleocapsid, viral protein
• Biological source: Vesicular stomatitis Indiana virus (VSIV)
• Cellular location: Virion: P03521
• Total number of polymer chains: 5
• Total formula weight: 240714.17

Authors

Luo, M.,Green, T.J.,Rowse, M. (deposition date: 2010-12-03, release date: 2011-01-12, Last modification date: 2024-02-21)

Primary citation

Green, T.J.,Rowse, M.,Tsao, J.,Kang, J.,Ge, P.,Zhou, Z.H.,Luo, M.
Access to RNA Encapsidated in the Nucleocapsid of Vesicular Stomatitis Virus.
J.Virol., 85:2714-2722, 2011

PubMed Abstract: The genomic RNA of negative-strand RNA viruses, such as vesicular stomatitis virus (VSV), is completely enwrapped by the nucleocapsid protein (N) in every stage of virus infection. During viral transcription/replication, however, the genomic RNA in the nucleocapsid must be accessible by the virus-encoded RNA-dependent RNA polymerase in order to serve as the template for RNA synthesis. With the VSV nucleocapsid and a nucleocapsid-like particle (NLP) produced in Escherichia coli, we have found that the RNA in the VSV nucleocapsid can be removed by RNase A, in contrast to what was previously reported. Removal of the RNA did not disrupt the assembly of the N protein, resulting in an empty capsid. Polyribonucleotides were reencapsidated into the empty NLP, and the crystal structures were determined. The crystal structures revealed variable degrees of association of the N protein with a specific RNA sequence.

PubMed: 21177817
DOI: 10.1128/JVI.01927-10

Experimental method

X-RAY DIFFRACTION (3.008 Å)