1i5p
From Proteopedia
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- | [[Image:1i5p.gif|left|200px]] | + | [[Image:1i5p.gif|left|200px]] |
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- | '''INSECTICIDAL CRYSTAL PROTEIN CRY2AA''' | + | {{Structure |
+ | |PDB= 1i5p |SIZE=350|CAPTION= <scene name='initialview01'>1i5p</scene>, resolution 2.20Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= CRY2AA OPERON ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29339 Bacillus thuringiensis serovar kurstaki]) | ||
+ | }} | ||
+ | |||
+ | '''INSECTICIDAL CRYSTAL PROTEIN CRY2AA''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1I5P is a [ | + | 1I5P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_kurstaki Bacillus thuringiensis serovar kurstaki]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5P OCA]. |
==Reference== | ==Reference== | ||
- | Structure of Cry2Aa suggests an unexpected receptor binding epitope., Morse RJ, Yamamoto T, Stroud RM, Structure. 2001 May 9;9(5):409-17. PMID:[http:// | + | Structure of Cry2Aa suggests an unexpected receptor binding epitope., Morse RJ, Yamamoto T, Stroud RM, Structure. 2001 May 9;9(5):409-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11377201 11377201] |
[[Category: Bacillus thuringiensis serovar kurstaki]] | [[Category: Bacillus thuringiensis serovar kurstaki]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lectin-like beta sandwich]] | [[Category: lectin-like beta sandwich]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:52 2008'' |
Revision as of 09:45, 20 March 2008
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, resolution 2.20Å | |||||||
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Gene: | CRY2AA OPERON (Bacillus thuringiensis serovar kurstaki) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
INSECTICIDAL CRYSTAL PROTEIN CRY2AA
Overview
BACKGROUND: Genetically modified (GM) crops that express insecticidal protein toxins are an integral part of modern agriculture. Proteins produced by Bacillus thuringiensis (Bt) during sporulation mediate the pathogenicity of Bt toward a spectrum of insect larvae whose breadth depends upon the Bt strain. These transmembrane channel-forming toxins are stored in Bt as crystalline inclusions called Cry proteins. These proteins are the active agents used in the majority of biorational pesticides and insect-resistant transgenic crops. Though Bt toxins are promising as a crop protection alternative and are ecologically friendlier than synthetic organic pesticides, resistance to Bt toxins by insects is recognized as a potential limitation to their application. RESULTS: We have determined the 2.2 A crystal structure of the Cry2Aa protoxin by multiple isomorphous replacement. This is the first crystal structure of a Cry toxin specific to Diptera (mosquitoes and flies) and the first structure of a Cry toxin with high activity against larvae from two insect orders, Lepidoptera (moths and butterflies) and Diptera. Cry2Aa also provides the first structure of the proregion of a Cry toxin that is cleaved to generate the membrane-active toxin in the larval gut. CONCLUSIONS: The crystal structure of Cry2Aa reported here, together with chimeric-scanning and domain-swapping mutagenesis, defines the putative receptor binding epitope on the toxin and so may allow for alteration of specificity to combat resistance or to minimize collateral effects on nontarget species. The putative receptor binding epitope of Cry2Aa identified in this study differs from that inferred from previous structural studies of other Cry toxins.
About this Structure
1I5P is a Single protein structure of sequence from Bacillus thuringiensis serovar kurstaki. Full crystallographic information is available from OCA.
Reference
Structure of Cry2Aa suggests an unexpected receptor binding epitope., Morse RJ, Yamamoto T, Stroud RM, Structure. 2001 May 9;9(5):409-17. PMID:11377201
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