TY - JOUR
T1 - High-Resolution Crystal Structure of Activated Cyt2Ba Monomer from Bacillus thuringiensis subsp. israelensis
AU - Cohen, Shmuel
AU - Dym, Orly
AU - Albeck, Shira
AU - Ben-Dov, Eitan
AU - Cahan, Rivka
AU - Firer, Michael
AU - Zaritsky, Arieh
N1 - Funding Information:
We thank Prof. Joel L. Sussman for helpful discussions. We are grateful to Anna Branzburg and Yigal Michael from the Israel Structural Proteomics Center for their skilled assistance. The structure was determined at the Israel Structural Proteomics Center, supported by The Israel Ministry of Science, Culture and Sport; the Divadol Foundation; the Neuman Foundation; and the European Commission Sixth Framework Research and Technological Development Programme ‘SPINE2-COMPLEXES’ Project under Contract No. 031220. Partial support was awarded by a grant (No. 2001-042) from the US–Israel Binational Science Foundation, Jerusalem, Israel (to A.Z.).
PY - 2008/7/25
Y1 - 2008/7/25
N2 - The Cyt family of proteins consists of δ-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 δ-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.
AB - The Cyt family of proteins consists of δ-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 δ-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.
KW - Cyt toxins
KW - X-ray crystal structure
KW - activated Cyt2Ba
KW - insecticidal crystal proteins
KW - membrane-active cytotoxin
UR - https://www.scopus.com/pages/publications/45949087915
U2 - 10.1016/j.jmb.2008.05.010
DO - 10.1016/j.jmb.2008.05.010
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C2 - 18571667
AN - SCOPUS:45949087915
SN - 0022-2836
VL - 380
SP - 820
EP - 827
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 5
ER -