Structural requirements of the unique disulphide bond and the proline-rich motif within the α4-α5 loop for larvicidal activity of the Bacillus thuringiensis Cry4Aa δ-endotoxin

• Main Authors: Satita Tapaneeyakorn, Walairat Pornwiroon, Gerd Katzenmeier, Chanan Angsuthanasombat
• Other Authors: Mahidol University
• Format: Article
• Published: 2018
• Subjects: Biochemistry, Genetics and Molecular Biology
• Online Access: https://repository.li.mahidol.ac.th/handle/123456789/16346

Both the disulphide bond (Cys192-Cys199) and the proline-rich motif (Pro193ProAsnPro196) in the long loop connecting the α4-α5 transmembrane hairpin of the Cry4Aa mosquito-larvicidal protein have been found to be unique among the Bacillus thuringiensis Cry δ-endotoxins. In this study, their structur...