1I5P
INSECTICIDAL CRYSTAL PROTEIN CRY2AA
Summary for 1I5P
| Entry DOI | 10.2210/pdb1i5p/pdb |
| Descriptor | PESTICIDIAL CRYSTAL PROTEIN CRY2AA (2 entities in total) |
| Functional Keywords | helical bundle, beta prism, lectin-like beta sandwich, jelly roll, toxin |
| Biological source | Bacillus thuringiensis serovar kurstaki |
| Total number of polymer chains | 1 |
| Total formula weight | 70907.95 |
| Authors | Morse, R.J.,Stroud, R.M.,Yamamoto, T. (deposition date: 2001-02-28, release date: 2001-05-16, Last modification date: 2024-10-30) |
| Primary citation | Morse, R.J.,Yamamoto, T.,Stroud, R.M. Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure, 9:409-417, 2001 Cited by PubMed Abstract: 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. PubMed: 11377201DOI: 10.1016/S0969-2126(01)00601-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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