Abstract

Urease is an enzyme which catalyses hydrolysis of urea to ammonia and carbon dioxide. Plant ureases but not bacterial ureases display insecticidal activity against insects with cathepsin B- and D-based digestive systems. It was found that a 10-kDa internal region of a plant urease exhibits this insecticidal activity, and more precisely it was predicted that a β-hairpin motif within this region may be responsible for this activity by functioning as a membrane pore former. We carried out molecular dynamics study of the jack bean urease insecticidal region in the presence of explicit water and in water/hexane interface, in order to gain more insight into the structural changes and behaviour of the hairpin region in the membrane-like interfacial environment. The results indicate that the hairpin anchors well in the polar/non-polar interface. Subsequent modelling study of the insecticidal region clearly suggests that this region can form a β-barrel assembly and thus supports our previous hypothesis that the insecticidal activity of plant ureases occurs through pore-forming β-barrel assembly.

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