Abstract
The 3.0 A resolution crystal structure of Pariacoto virus (PaV) reveals extensive interactions between portions of the viral RNA genome and the icosahedral capsid. Under the protein shell of the T = 3 quasi equivalent capsid lies a dodecahedral cage composed of RNA duplex that accounts for approximately 35% of the single-stranded RNA genome. The highly basic N-terminal regions (residues 7-54) of the subunits, forming pentamers (A subunits) are clearly visible in the density map and make numerous interactions with the RNA cage. The C-terminal segments (residues 394-401) of the A subunits lie in channels near the quasi three-fold axes. Electron cryo-microscopy and image reconstruction of PaV particles clearly show the dodecahedral RNA cage.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Capsid / chemistry
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Capsid / genetics
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Capsid / metabolism
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Capsid / ultrastructure
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Cryoelectron Microscopy
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Crystallography, X-Ray
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Genome, Viral
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Insect Viruses / chemistry
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Insect Viruses / genetics*
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Insect Viruses / ultrastructure*
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Nucleic Acid Conformation
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Subunits
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RNA Viruses / chemistry
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RNA Viruses / genetics*
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RNA Viruses / ultrastructure*
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RNA, Viral / chemistry
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RNA, Viral / genetics
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RNA, Viral / ultrastructure*
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Sequence Alignment
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Spodoptera / virology*
Substances
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Protein Subunits
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RNA, Viral