Delta endotoxin
From Wikipedia, the free encyclopedia
| delta endotoxin | ||
|---|---|---|
| Identifiers | ||
| Symbol | Endotoxin_M | |
| Pfam | PF00555 | |
| InterPro | IPR015790 | |
| SCOP | 1dlc | |
| TCDB | 1.C.2 | |
| OPM family | 95 | |
| OPM protein | 1w99 | |
| Available PDB structures: | ||
Delta endotoxins are insecticidal toxins produced by Bacillus species of bacteria.
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 (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[1][2].
[edit] References
- ^ Cygler M, Borisova S, Grochulski P, Masson L, Pusztai-carey M, Schwartz JL, Brousseau R (1995). "Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation". J. Mol. Biol. 254 (3): 447–464. doi:. PMID 7490762.
- ^ Ghosh D, Pangborn W, Galitsky N, Cody V, Wojtczak A, Luft JR, English L (2001). "Structure of the insecticidal bacterial delta-endotoxinCry3Bb1 of Bacillus thuringiensis". Acta Crystallogr. D 57: 1101–1109. doi:. PMID 11468393.
This article includes text from the public domain Pfam and InterPro IPR015790
