White, Helen E. and Sherman, M.B. and Brasiles, S. and Jacquet, E. and Seavers, P. and Tavares, P. and Orlova, Elena (2012) Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly. Journal of Virology 86 (12), pp. 6768-6777. ISSN 0022-538X.Full text not available from this repository.
The structure of bacteriophage SPP1 capsid was determined at sub-nanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major capsid protein gp13 and the auxiliary protein gp12 that are organized in a T=7 lattice. DNA is arranged in layers with a distance of ∼24.5 Å. Gp12 forms spikes that are anchored at the centre of gp13 hexamers. In a gp12-deficient mutant the centres of hexamers are closed by loops of gp13 coming together to protect the SPP1 genome from the outside environment. The HK97-like fold was used to build a pseudo-atomic model of gp13. Its structural organization remains unchanged upon tail binding and following DNA release. Gp13 exhibits enhanced thermostability in the DNA-filled capsid. A remarkable convergence between thermostability of the capsid and of the other virion components was found, revealing that the overall architecture of the SPP1 infectious particle co-evolved towards high robustness.
|School or Research Centre:||Birkbeck Schools and Research Centres > School of Science > Biological Sciences|
|Date Deposited:||23 Apr 2012 10:17|
|Last Modified:||06 Oct 2016 10:15|
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