The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins.

Alexey DementievJason BoardAnand SitaramTimothy HeyMatthew S KelkerXiaoping XuYan HuCristian Vidal-QuistVimbai ChikwanaSamantha GriffinDavid McCaskillNick X WangShao-Ching HungMichael K ChanMarianne M LeeJessica HughesAlice WegenerRaffi V AroianKenneth E NarvaColin Berry

Published in: BMC biology (2016)

Cry6 proteins are members of the alpha helical pore-forming toxins - a structural class not previously recognized among the Cry toxins of B. thuringiensis and representing a new paradigm for nematocidal and insecticidal proteins. Elucidation of both the structure and the pore-forming mechanism of action of Cry6Aa now opens the way to more detailed analysis of toxin specificity and the development of new toxin variants with novel activities.

Keyphrases

escherichia coli
copy number
gene expression
bacillus subtilis