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Aerolysin and pertussis toxin share a common receptor‐binding domain
Author(s) -
Rossjohn Jamie,
Buckley J.Thomas,
Hazes Bart,
Murzin Alexey G.,
Read Randy J.,
Parker Michael W.
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.12.3426
Subject(s) - parade , microbial toxins , library science , biology , history , art history , microbiology and biotechnology , toxin , computer science
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 three‐stranded antiparallel β‐sheets that come together and 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 be 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.