| Literature DB >> 18571667 |
Shmuel Cohen1, Orly Dym, Shira Albeck, Eitan Ben-Dov, Rivka Cahan, Michael Firer, Arieh Zaritsky.
Abstract
The Cyt family of proteins consists of delta-endotoxins expressed during sporulation of several subspecies of Bacillus thuringiensis. Its members possess insecticidal, hemolytic, and cytolytic activities through pore formation and attract attention due to their potential use as vehicles for targeted membrane destruction. The delta-endotoxins of subsp. israelensis include three Cyt species: a major Cyt1Aa and two minor proteins, Cyt2Ba and Cyt1Ca. A cleaved Cyt protein that lacks the N- and C-terminal segments forms a toxic monomer. Here, we describe the crystal structure of Cyt2Ba, cleaved at its amino and carboxy termini by bacterial endogenous protease(s). Overall, its fold resembles that of the previously described volvatoxin A2 and the nontoxic form of Cyt2Aa. The structural similarity between these three proteins may provide information regarding the mechanism(s) of membrane-perforating toxins.Entities:
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Year: 2008 PMID： 18571667 DOI： 10.1016/j.jmb.2008.05.010
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469