Aerolysin and pertussis toxin share a common receptor-binding domain

被引:48
作者
Rossjohn, J
Buckley, JT
Hazes, B
Murzin, AG
Read, RJ
Parker, MW
机构
[1] ST VINCENTS INST MED RES, IAN POTTER FDN PROT CRYSTALLOG LAB, FITZROY, VIC 3065, AUSTRALIA
[2] UNIV VICTORIA, DEPT BIOCHEM & MICROBIOL, VICTORIA, BC V8W 2Y2, CANADA
[3] UNIV ALBERTA, DEPT MED MICROBIOL & IMMUNOL, EDMONTON, AB T6G 2H7, CANADA
[4] MRC CTR, CTR PROT ENGN, CAMBRIDGE CB2 2QH, ENGLAND
基金
英国惠康基金;
关键词
aerolysin; carbohydrate binding; C-type lectins; pertussis toxin; toxins;
D O I
10.1093/emboj/16.12.3426
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
We have discovered that the bacterial toxins aerolysin and pertussis toxin share a common domain. This is surprising because the two toxins affect cells in very different ways. The common domain, which we call the APT domain, consists of two free-stranded antiparallel beta-sheets that come together acid wrap around a central pair of helices. The APT domain shares a common fold with the C-type lectins and Link modules, and there appears to be a divergent relationship among the three families. One surface region of the APT domain is highly conserved, raising the possibility that the domains have a common function in both proteins. Mutation of one of the conserved surface residues in aerolysin, Tyr61, results in reduced receptor binding and activity, thus providing, evidence that the APT domain may he involved in interaction with the toxin's receptor Structural and biochemical evidence suggests that the APT domain contains a carbohydrate-binding site that can direct the toxins to their target cells.
引用
收藏
页码:3426 / 3434
页数:9
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