Structural highlights
Function
[CAPSD_BPT5] Major capsid protein that self-associates to form 120 hexamers and 11 pentamers, building the T=13 icosahedral capsid which about 860 Angstroms in diameter. Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function. The capsid gains its final stability through the reorganization of the subunits that takes place upon expansion. DNA encapsidation through the portal triggers capsid expansion and the binding of the decoration protein to the capsid exterior.[1] [2] [3]
References
- ↑ Huet A, Conway JF, Letellier L, Boulanger P. In vitro assembly of the T=13 procapsid of bacteriophage T5 with its scaffolding domain. J Virol. 2010 Sep;84(18):9350-8. doi: 10.1128/JVI.00942-10. Epub 2010 Jun 23. PMID:20573812 doi:https://dx.doi.org/10.1128/JVI.00942-10
- ↑ Preux O, Durand D, Huet A, Conway JF, Bertin A, Boulogne C, Drouin-Wahbi J, Trevarin D, Perez J, Vachette P, Boulanger P. A two-state cooperative expansion converts the procapsid shell of bacteriophage T5 into a highly stable capsid isomorphous to the final virion head. J Mol Biol. 2013 Jun 12;425(11):1999-2014. doi: 10.1016/j.jmb.2013.03.002. Epub, 2013 Mar 13. PMID:23500494 doi:https://dx.doi.org/10.1016/j.jmb.2013.03.002
- ↑ Huet A, Duda RL, Hendrix RW, Boulanger P, Conway JF. Correct Assembly of the Bacteriophage T5 Procapsid Requires Both the Maturation Protease and the Portal Complex. J Mol Biol. 2016 Jan 16;428(1):165-81. doi: 10.1016/j.jmb.2015.11.019. Epub 2015 , Nov 23. PMID:26616586 doi:https://dx.doi.org/10.1016/j.jmb.2015.11.019
