2RCI

High-resolution crystal structure of activated Cyt2Ba monomer from Bacillus thuringiensis subsp. israelensis

Summary for 2RCI

• Entry DOI: 10.2210/pdb2rci/pdb
• Descriptor: Type-2Ba cytolytic delta-endotoxin (2 entities in total)
• Functional Keywords: alpha/beta architecture with beta-sheet surrounded by two alpha-helix layers, structural genomics, israel structural proteomics center, ispc, plasmid, sporulation, toxin
• Biological source: Bacillus thuringiensis serovar israelensis
• Total number of polymer chains: 1
• Total formula weight: 22973.14

Authors

Dym, O.,Israel Structural Proteomics Center (ISPC) (deposition date: 2007-09-20, release date: 2008-07-15, Last modification date: 2023-08-30)

Primary citation

Cohen, S.,Dym, O.,Albeck, S.,Ben-Dov, E.,Cahan, R.,Firer, M.,Zaritsky, A.
High-resolution crystal structure of activated Cyt2Ba monomer from Bacillus thuringiensis subsp. israelensis.
J.Mol.Biol., 380:820-827, 2008

PubMed 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.

PubMed: 18571667
DOI: 10.1016/j.jmb.2008.05.010

Experimental method

X-RAY DIFFRACTION (1.8 Å)