His¹⁸⁰ in the pore-lining α4 of the Bacillus thuringiensis Cry4Aa δ-endotoxin is crucial for structural arrangements of the α4-α5 transmembrane hairpin and hence biotoxicity

• Main Authors: Walairat Bourchookarn, Apichai Bourchookarn, Chompounoot Imtong, Hui Chun Li, Chanan Angsuthanasombat
• Other Authors: Tzu Chi University
• Format: Article
• Published: 2022
• Subjects: Biochemistry, Genetics and Molecular Biology; Chemistry
• Online Access: https://repository.li.mahidol.ac.th/handle/123456789/76172
• Institution: Mahidol University

One proposed toxic mechanism of Bacillus thuringiensis Cry δ-endotoxins involves pore formation in target membranes by the α4-α5 transmembrane hairpin constituting their pore-forming domain. Here, nine selected charged and uncharged polar residues in the pore-lining α4 of the Cry4Aa mosquito-active...