Publication details

Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins

Authors

KOMÁREK Jan KAVKOVÁ Eva HOUSER Josef HORÁČKOVÁ Aneta HOLKOVÁ Jitka DEMO Gabriel WIMMEROVÁ Michaela

Year of publication 2018
Type Article in Periodical
Magazine / Source Proteins : structure, function, and genetics
MU Faculty or unit

Faculty of Science

Citation
Web https://onlinelibrary.wiley.com/doi/full/10.1002/prot.25522
Doi http://dx.doi.org/10.1002/prot.25522
Keywords Agaricus bisporus; bacterial toxins; protein stability; protein structure; toxin-like proteins
Description We report the characterization of the dimeric protein AB21 from Agaricus bisporus, one of the most commonly and widely consumed mushrooms in the world. The protein shares no significant sequence similarity with any protein of known function, and it is the first characterized member of its protein family. The coding sequence of the ab21 gene was determined and the protein was expressed in E. coli in a recombinant form. We demonstrated a high thermal and pH stability of AB21 and proved the weak affinity of the protein to divalent ions of some transition metals (nickel, zinc, cadmium, and cobalt). The reported crystallographic structure exhibits an interesting rodlike helical bundle fold with structural similarity to bacterial toxins of the ClyA superfamily. By immunostaining, we demonstrated an abundance of AB21 in the fruiting bodies of A. bisporus.
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