Restriction of intramolecular movements within the Cry1Aa toxin molecule of Bacillus thuringiensis through disulfide bond engineering.

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 Lett

journal_title

FEBS letters

authors

Schwartz JL,Juteau M,Grochulski P,Cygler M,Préfontaine G,Brousseau R,Masson L

doi

10.1016/s0014-5793(97)00626-1

subject

Has Abstract

pub_date

1997-06-30 00:00:00

pages

397-402

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00626-1

journal_volume

410

pub_type

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