FEATURES

FAMILY

Tevenvirinae major capsid protein family

DESCRIPTION

Also known as CAPSH_BPT4, gp23. Major capsid protein that self-associates to form hexamers, building most of the capsid in association with pentons made of the capsid vertex protein and one dodecamer of the portal protein. The major capsid protein self-associates to form 160 hexamers, building most of the T=13 laevo capsid. Folding of major capsid protein 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. Homohexamer. Interacts with the portal protein. Interacts with the capsid vertex protein that forms pentamers. Interacts with hoc; one hoc molecule associates with each capsid hexamer. Interacts with soc; this interaction reinforces the capsid structure. A total of 960 subunits of the major capsid protein forms the 160 hexamers.

EXTERNAL LINKS

gp23

Structural Ligandability

Domains Chains

Distribution