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

J. Komárek, E. Ivanov Kavková, J. Houser, A. Horáčková, J. Ždánská, G. Demo, M. Wimmerová,

. 2018 ; 86 (9) : 897-911. [pub] 20180520

Language English Country United States

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc19035269

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 rod-like 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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$a Komárek, Jan $u Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
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$a Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins / $c J. Komárek, E. Ivanov Kavková, J. Houser, A. Horáčková, J. Ždánská, G. Demo, M. Wimmerová,
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$a 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 rod-like 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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$a Ivanov Kavková, Eva $u Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
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$a Houser, Josef $u Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
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$a Horáčková, Aneta $u Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
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$a Ždánská, Jitka $u Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic.
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$a Demo, Gabriel $u Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
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$a Wimmerová, Michaela $u Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic. Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
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