Structural highlights
Function
CAPSH_BPT4 Major capsid protein that self-associates to form 160 hexamers, building most of the T=13 laevo capsid in association with 11 pentons made of gp24 and one dodecamer of gp20. Folding of gp23 requires the assistance of two chaperones, the host chaperone groL acting with the phage encoded gp23-specific chaperone, gp31. The capsid also contains two nonessential outer capsid proteins, Hoc and Soc, which decorate the capsid surface. Through binding to adjacent gp23 subunits, Soc reinforces the capsid structure.[1] [2]
References
- ↑ Fokine A, Chipman PR, Leiman PG, Mesyanzhinov VV, Rao VB, Rossmann MG. Molecular architecture of the prolate head of bacteriophage T4. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6003-8. Epub 2004 Apr 7. PMID:15071181 doi:https://dx.doi.org/10.1073/pnas.0400444101
- ↑ Aebi U, Bijlenga R, v d Broek J, v d Broek H, Eiserling F, Kellenberger C, Kellenberger E, Mesyanzhinov V, Muller L, Showe M, Smith R, Steven A. The transformation of tau particles into T4 heads. II. Transformations of the surface lattice and related observations on form determination. J Supramol Struct. 1974;2(2-4):253-75. PMID:4612249 doi:https://dx.doi.org/10.1002/jss.400020218
