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

被引：42

作者：

Cohen, Shmuel ^{[1
,2
]}

Dym, Orly ^{[3
]}

Albeck, Shira ^{[3
]}

Ben-Dov, Eitan ^{[1
,4
]}

Cahan, Rivka ^{[2
]}

Firer, Michael ^{[2
]}

Zaritsky, Arieh ^{[1
]}

机构：

[1] Ben Gurion Univ Negev, Dept Life Sci, IL-84105 Beer Sheva, Israel

[2] Ariel Univ Ctr Samaria, Dept Chem Engn & Biotechnol, IL-40700 Ariel, Israel

[3] Weizmann Inst Sci, ISPC, IL-76100 Rehovot, Israel

[4] Achva Acad Coll, IL-78900 Mobile Post Shikmim, Israel

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2008年 / 380卷 / 05期

关键词：

Cyt toxins; activated Cyt2Ba; insecticidal crystal proteins; membrane-active cytotoxin; X-ray crystal structure;

D O I：

10.1016/j.jmb.2008.05.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：820 / 827

页数：8

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