2rci
From Proteopedia
High-resolution crystal structure of activated Cyt2Ba monomer from Bacillus thuringiensis subsp. israelensis
Structural highlights
FunctionCT2BA_BACTI Kills the larvae of dipteran insects by making pores in the epithelial cell membrane of the insect midgut (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. High-resolution crystal structure of activated Cyt2Ba monomer from Bacillus thuringiensis subsp. israelensis.,Cohen S, Dym O, Albeck S, Ben-Dov E, Cahan R, Firer M, Zaritsky A J Mol Biol. 2008 Jul 25;380(5):820-7. Epub 2008 May 11. PMID:18571667[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||
