6DJ4

Crystal Structure of Bacillus thuringiensis Cry1A.105 Tryptic Core

Summary for 6DJ4

• Entry DOI: 10.2210/pdb6dj4/pdb
• Descriptor: Cry1A.105 (2 entities in total)
• Functional Keywords: pesticidal crystal protein, toxin
• Biological source: Bacillus thuringiensis; More
• Total number of polymer chains: 1
• Total formula weight: 66539.27

Authors

Rydel, T.J.,Sturman, E.J.,Lee, T.C. (deposition date: 2018-05-24, release date: 2018-09-12, Last modification date: 2024-04-03)

Primary citation

Wang, C.,Li, W.,Kessenich, C.R.,Petrick, J.S.,Rydel, T.J.,Sturman, E.J.,Lee, T.C.,Glenn, K.C.,Edrington, T.C.
Safety of the Bacillus thuringiensis-derived Cry1A.105 protein: Evidence that domain exchange preserves mode of action and safety.
Regul. Toxicol. Pharmacol., 99:50-60, 2018

PubMed Abstract: The lepidopteran-active Cry1A.105 protein is a chimeric three-domain insecticidal toxin with distinct structural domains derived from the naturally occurring Cry1Ab, Cry1Ac and Cry1F proteins from the soil bacterium Bacillus thuringiensis (Bt). The X-ray crystal structure of the Cry1A.105 tryptic core at 3.0 Å resolution demonstrates its high structural similarity to the tryptic core of Cry1Ac. Bioinformatics analyses demonstrate that Cry1A.105 has no significant amino acid sequence similarity to known allergens or mammalian toxins, which is the same conclusion reached for its component domains. Like its intact donor proteins, Cry1A.105 was heat labile at temperatures ≥75 °C and degraded upon exposure to gastrointestinal proteases. No adverse effects were observed in mice when Cry1A.105 was dosed orally at 2451 mg/kg body weight. Therefore, the weight of evidence supports that Cry1A.105 is safe for human and animal consumption. These results support the conclusion that the safety of a chimeric protein for human or animal consumption can be evaluated in the context of the safety of its donor proteins.

PubMed: 30196079
DOI: 10.1016/j.yrtph.2018.09.003

Experimental method

X-RAY DIFFRACTION (3.01 Å)