| Description | The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production [ ]. 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 () involved in membrane insertion and pore formation; a β-sheet central domain involved in receptor binding; and a C-terminal β-sandwich domain ( ) that interacts with the N-terminal domain to form a channel [ , ].This entry represents the central β-sheet domain superfamily, which consists of three four-stranded β-sheets, each with a Greek key fold, with internal pseudo threefold symmetry. Thus, it acts as a receptor binding β-prism, binding to insect-specific receptors of gut epithelial cells [ ]. | Name | Pesticidal crystal protein, central domain superfamily |
| Short Name | Pest_cryst_cen_dom_sf | Type | Homologous_superfamily |
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