1dlc
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlc OCA], [http://www.ebi.ac.uk/pdbsum/1dlc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dlc RCSB]</span> | ||
}} | }} | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:46 2008'' |
Revision as of 16:43, 30 March 2008
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, resolution 2.5Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF INSECTICIDAL DELTA-ENDOTOXIN FROM BACILLUS THURINGIENSIS AT 2.5 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1DLC is a Single protein structure of sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA.
Reference
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
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