Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
29722060
DOI
10.1002/prot.25522
Knihovny.cz E-resources
- Keywords
- Agaricus bisporus, bacterial toxins, protein stability, protein structure, toxin-like proteins,
- MeSH
- Agaricus chemistry MeSH
- Bacterial Toxins chemistry MeSH
- Pore Forming Cytotoxic Proteins biosynthesis chemistry genetics MeSH
- Escherichia coli genetics metabolism MeSH
- Fungal Proteins biosynthesis chemistry genetics MeSH
- Cations, Divalent chemistry MeSH
- Protein Conformation MeSH
- Transition Elements chemistry MeSH
- Recombinant Proteins biosynthesis chemistry genetics MeSH
- Protein Folding MeSH
- Protein Stability MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Toxins MeSH
- Pore Forming Cytotoxic Proteins MeSH
- Fungal Proteins MeSH
- Cations, Divalent MeSH
- Transition Elements MeSH
- Recombinant Proteins MeSH
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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