Abstract:
:Disulfide bridges were introduced into CrylAa, a Bacillus thuringiensis lepidopteran toxin, to stabilize different protein domains including domain I alpha-helical regions thought to be involved in membrane integration and permeation. Bridged mutants could not form functional ion channels in lipid bilayers in the oxidized state, but upon reduction with beta-mercaptoethanol, regained parental toxin channel activity. Our results show that unfolding of the protein around a hinge region linking domain I and II is a necessary step for pore formation. They also suggest that membrane insertion of the hydrophobic hairpin made of alpha-helices 4 and 5 in domain I plays a critical role in the formation of a functional pore.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Schwartz JL,Juteau M,Grochulski P,Cygler M,Préfontaine G,Brousseau R,Masson Ldoi
10.1016/s0014-5793(97)00626-1subject
Has Abstractpub_date
1997-06-30 00:00:00pages
397-402issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00626-1journal_volume
410pub_type
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