delta endotoxin, N-terminal domain | |||||||||
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crystal structure of the insecticidal bacterial del endotoxin Cry3Bb1 bacillus thuringiensis
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Identifiers | |||||||||
Symbol | Endotoxin_N | ||||||||
Pfam | PF03945 | ||||||||
InterPro | IPR005639 | ||||||||
SCOP | 1dlc | ||||||||
SUPERFAMILY | 1dlc | ||||||||
TCDB | 1.C.2 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
delta endotoxin | |||||||||
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Structure of insecticidal delta-endotoxin from Bacillus thuringiensis.
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Identifiers | |||||||||
Symbol | Endotoxin_M | ||||||||
Pfam | PF00555 | ||||||||
InterPro | IPR015790 | ||||||||
SCOP | 1dlc | ||||||||
SUPERFAMILY | 1dlc | ||||||||
TCDB | 1.C.2 | ||||||||
OPM superfamily | 95 | ||||||||
OPM protein | 1w99 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Bacillus thuringiensis delta-Endotoxin, middle domain | |||||||||
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insecticidal crystal protein cry2aa
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Identifiers | |||||||||
Symbol | Endotoxin_mid | ||||||||
Pfam | PF09131 | ||||||||
InterPro | IPR015214 | ||||||||
SCOP | 1i5p | ||||||||
SUPERFAMILY | 1i5p | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
delta endotoxin | |||||||||
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insecticidal crystal protein cry2aa
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Identifiers | |||||||||
Symbol | Endotoxin_C | ||||||||
Pfam | PF03944 | ||||||||
Pfam clan | CL0202 | ||||||||
InterPro | IPR005638 | ||||||||
SCOP | 1dlc | ||||||||
SUPERFAMILY | 1dlc | ||||||||
TCDB | 1.C.2 | ||||||||
CDD | cd04085 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Delta endotoxins (δ-endotoxins, also called Cry and Cyt toxins) are pore-forming toxins produced by Bacillus thuringiensis species of bacteria. They are useful for their insecticidal action.
During spore formation the bacteria produce crystals of this protein. 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 delta toxin is composed of three distinct structural domains: an N-terminal helical bundle domain (InterPro: IPR005639) involved in membrane insertion and pore formation; a beta-sheet central domain involved in receptor binding; and a C-terminal beta-sandwich domain (InterPro: IPR005638) that interacts with the N-terminal domain to form a channel.
This article incorporates text from the public domain Pfam and InterPro IPR015790