Summary: Bacillus thuringiensis delta-Endotoxin, middle domain
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Delta endotoxin Edit Wikipedia article
|delta endotoxin, N-terminal domain|
crystal structure of the insecticidal bacterial del endotoxin Cry3Bb1 bacillus thuringiensis
Structure of insecticidal delta-endotoxin from Bacillus thuringiensis.
|Bacillus thuringiensis delta-Endotoxin, middle domain|
insecticidal crystal protein cry2aa
insecticidal crystal protein cry2aa
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.
- Li JD, Carroll J, Ellar DJ (October 1991). "Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 A resolution". Nature 353 (6347): 815–21. doi:10.1038/353815a0. PMID 1658659.
- 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:10.1006/jmbi.1995.0630. 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 (8): 1101–1109. doi:10.1107/S0907444901008186. PMID 11468393.
- Grochulski P, Masson L, Borisova S, Pusztai-Carey M, Schwartz JL, Brousseau R, Cygler M (December 1995). "Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation". J. Mol. Biol. 254 (3): 447–64. doi:10.1006/jmbi.1995.0630. PMID 7490762.
- Galitsky N, Cody V, Wojtczak A, Ghosh D, Luft JR, Pangborn W, English L (August 2001). "Structure of the insecticidal bacterial delta-endotoxin Cry3Bb1 of Bacillus thuringiensis". Acta Crystallogr. D Biol. Crystallogr. 57 (Pt 8): 1101–9. doi:10.1107/S0907444901008186. PMID 11468393.
- Bravo, A.; Gill, S. S.; Soberón, M. (2007). "Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control". Toxicon 49 (4): 423–435. doi:10.1016/j.toxicon.2006.11.022. PMC 1857359. PMID 17198720.
- Pigott, C. R.; Ellar, D. J. (2007). "Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity". Microbiology and Molecular Biology Reviews 71 (2): 255–281. doi:10.1128/MMBR.00034-06. PMC 1899880. PMID 17554045.
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Bacillus thuringiensis delta-Endotoxin, middle domain Provide feedback
Members of this family adopt a structure consisting of three four-stranded beta-sheets, each with a Greek key fold, with internal pseudo threefold symmetry. Thus they act as a receptor binding beta-prism, binding to insect-specific receptors of gut epithelial cells .
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This tab holds annotation information from the InterPro database.
InterPro entry IPR015214
Many Bacillus species produce crystals of insecticidal toxins during spore formation. 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) involved in membrane insertion and pore formation; a beta-sheet central domain involved in receptor binding; and a C-terminal beta-sandwich domain (INTERPRO) that interacts with the N-terminal domain to form a channel [PUBMED:7490762, PUBMED:11468393].
This entry represents the central beta-sheet domain, which consistins of three four-stranded beta-sheets, each with a Greek key fold, with internal pseudo threefold symmetry. Thus, it acts as a receptor binding beta-prism, binding to insect-specific receptors of gut epithelial cells [PUBMED:11377201]. This entry is found almost exclusively in Bacillus thuringiensis.
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|Number in seed:||3|
|Number in full:||68|
|Average length of the domain:||192.60 aa|
|Average identity of full alignment:||70 %|
|Average coverage of the sequence by the domain:||32.83 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Endotoxin_mid domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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