Abstract
Vesicular stomatitis virus is a negative-stranded RNA virus. Its nucleoprotein (N) binds the viral genomic RNA and is involved in multiple functions including transcription, replication, and assembly. We have determined a 2.9 angstrom structure of a complex containing 10 molecules of the N protein and 90 bases of RNA. The RNA is tightly sequestered in a cavity at the interface between two lobes of the N protein. This serves to protect the RNA in the absence of polynucleotide synthesis. For the RNA to be accessed, some conformational change in the N protein should be necessary.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallography, X-Ray
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Hydrophobic and Hydrophilic Interactions
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Models, Molecular
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Molecular Sequence Data
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Nucleic Acid Conformation
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Nucleocapsid Proteins / chemistry*
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Nucleocapsid Proteins / metabolism
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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RNA, Viral / chemistry*
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RNA, Viral / metabolism
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Ribonucleoproteins / chemistry*
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Sequence Alignment
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Vesicular stomatitis Indiana virus / chemistry*
Substances
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Nucleocapsid Proteins
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RNA, Viral
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Ribonucleoproteins