Structural highlights
Function
[CR3AA_BACTT] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the delta-endotoxin from Bacillus thuringiensis subsp. tenebrionis that is specifically toxic to Coleoptera insects (beetle toxin) has been determined at 2.5 A resolution. It comprises three domains which are, from the N- to C-termini, a seven-helix bundle, a three-sheet domain, and a beta sandwich. The core of the molecule encompassing all the domain interfaces is built from conserved sequence segments of the active delta-endotoxins. Therefore the structure represents the general fold of this family of insecticidal proteins. The bundle of long, hydrophobic and amphipathic helices is equipped for pore formation in the insect membrane, and regions of the three-sheet domain are probably responsible for receptor binding.
Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 A resolution.,Li JD, Carroll J, Ellar DJ Nature. 1991 Oct 31;353(6347):815-21. PMID:1658659[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li JD, Carroll J, Ellar DJ. Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 A resolution. Nature. 1991 Oct 31;353(6347):815-21. PMID:1658659 doi:http://dx.doi.org/10.1038/353815a0
