Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1940079 | Biochemical and Biophysical Research Communications | 2006 | 6 Pages |
Abstract
We show herein that interaction in aqueous solution of the two components of binary toxin from Bacillus sphaericus, BinA and BinB, leads to a dramatic conformational change, from β turns or random coil, to β structure. Also, either BinA or BinB separately or their equimolar mixture, interact with lipid bilayers resulting in further conformational changes. Upon membrane association, the change in conformation observed for BinA or BinB separately is different from that observed when the proteins are combined, indicating that proper folding depends on the presence of the complementary subunit. We also show, in contrast to previous reports, that BinB, but not BinA, is able to insert in model neutral lipid monolayers.
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Authors
Panadda Boonserm, Seangduen Moonsom, Chanikarn Boonchoy, Boonhiang Promdonkoy, Krupakar Parthasarathy, Jaume Torres,