El_Omari_et_al_(2013).pdf (3.95 MB)
Plate tectonics of virus shell assembly and reorganization in phage f8, a distant relative of mammalian reoviruses
journal contribution
posted on 2023-06-08, 20:34 authored by Kamel El Omari, Geoff Sutton, Janne J Ravantti, Hanwen Zhang, Thomas S Walter, Jonathan M Grimes, Dennis H Bamford, David I Stuart, Erika ManciniErika ManciniThe hallmark of a virus is its capsid, which harbors the viral genome and is formed from protein subunits, which assemble following precise geometric rules. dsRNA viruses use an unusual protein multiplicity (120 copies) to form their closed capsids. We have determined the atomic structure of the capsid protein (P1) from the dsRNA cystovirus F8. In the crystal P1 forms pentamers, very similar in shape to facets of empty procapsids, suggesting an unexpected assembly pathway that proceeds via a pentameric intermediate. Unlike the elongated proteins used by dsRNA mammalian reoviruses, P1 has a compact trapezoid-like shape and a distinct arrangement in the shell, with two near-identical conformers in nonequivalent structural environments. Nevertheless, structural similarity with the analogous protein from the mammalian viruses suggests a common ancestor. The unusual shape of the molecule may facilitate dramatic capsid expansion during phage maturation, allowing P1 to switch interaction interfaces to provide capsid plasticity.
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Publication status
- Published
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- Published version
Journal
StructureISSN
1878-4186Publisher
Cell PressExternal DOI
Issue
8Volume
21Page range
1384-1395Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2015-04-23First Open Access (FOA) Date
2015-04-23First Compliant Deposit (FCD) Date
2015-04-23Usage metrics
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