1i5p

<table><tr><td colspan='2'>[[1i5p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bactk Bactk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1I5P FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRY2AA OPERON ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29339 BACTK])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1i5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5p OCA], [http://pdbe.org/1i5p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i5p RCSB], [http://www.ebi.ac.uk/pdbsum/1i5p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5p ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CR2AA_BACTK CR2AA_BACTK]] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of both dipteran (Aedes aegypti) and lepidopteran (Manduca sexta) larvae.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11377201</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bactk]]

[[Category: Morse, R J]]

[[Category: Stroud, R M]]

[[Category: Yamamoto, T]]

[[Category: Toxin]]