Domain

Pesticidal crystal protein, C-terminal (IPR005638)

Short name: Pest_crys_C

Overlapping homologous superfamilies

None.

Domain relationships

None.

Description

The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production [PMID: 9729610]. When an insect ingests these proteins, they are activated by proteolytic cleavage. The N terminus is cleaved in all of the proteins and a C-terminal extension is cleaved in some members. Once activated, the endotoxin binds to the gut epithelium and causes cell lysis by the formation of cation-selective channels, which leads to death. The activated region of the toxin is composed of three distinct structural domains: an N-terminal helical bundle domain (IPR005639) involved in membrane insertion and pore formation; a beta-sheet central domain involved in receptor binding; and a C-terminal beta-sandwich domain (IPR005638) that interacts with the N-terminal domain to form a channel [PMID: 7490762, PMID: 11468393].

This entry represents the conserved C-terminal domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0090729 toxin activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam