1dlc
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(New page: 200px<br /><applet load="1dlc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dlc, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 11:15, 20 November 2007
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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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