2C9K
Structure of the functional form of the mosquito-larvicidal Cry4Aa toxin from Bacillus thuringiensis at 2.8 A resolution
Summary for 2C9K
| Entry DOI | 10.2210/pdb2c9k/pdb |
| Descriptor | PESTICIDAL CRYSTAL PROTEIN CRY4AA, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total) |
| Functional Keywords | toxin, insect toxin, bioinsecticicide, pore formation, receptor recognition, sporulation |
| Biological source | BACILLUS THURINGIENSIS |
| Total number of polymer chains | 1 |
| Total formula weight | 70020.41 |
| Authors | Boonserm, P.,Mo, M.,Angsuthanasombat, C.,Lescar, J. (deposition date: 2005-12-13, release date: 2006-04-25, Last modification date: 2024-11-06) |
| Primary citation | Boonserm, P.,Mo, M.,Angsuthanasombat, C.,Lescar, J. Structure of the Functional Form of the Mosquito Larvicidal Cry4Aa Toxin from Bacillus Thuringiensis at 2.8-Angstrom Resolution. J.Bacteriol., 188:3391-, 2006 Cited by PubMed Abstract: The Cry4Aa delta-endotoxin from Bacillus thuringiensis is toxic to larvae of Culex, Anopheles, and Aedes mosquitoes, which are vectors of important human tropical diseases. With the objective of designing modified toxins with improved potency that could be used as biopesticides, we determined the structure of this toxin in its functional form at a resolution of 2.8 angstroms. Like other Cry delta-endotoxins, the activated Cry4Aa toxin consists of three globular domains, a seven-alpha-helix bundle responsible for pore formation (domain I) and the following two other domains having structural similarities with carbohydrate binding proteins: a beta-prism (domain II) and a plant lectin-like beta-sandwich (domain III). We also studied the effect on toxicity of amino acid substitutions and deletions in three loops located at the surface of the putative receptor binding domain II of Cry4Aa. Our results indicate that one loop is an important determinant of toxicity, presumably through attachment of Cry4Aa to the surface of mosquito cells. The availability of the Cry4Aa structure should guide further investigations aimed at the molecular basis of the target specificity and membrane insertion of Cry endotoxins. PubMed: 16621834DOI: 10.1128/JB.188.9.3391-3401.2006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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