6FPD
AB21 protein from Agaricus bisporus
Summary for 6FPD
| Entry DOI | 10.2210/pdb6fpd/pdb |
| Descriptor | Protein AB21, SODIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | agaricus bisporus, tetrahelical bundle, toxin-like, unknown function |
| Biological source | Agaricus bisporus |
| Total number of polymer chains | 1 |
| Total formula weight | 22657.18 |
| Authors | Houser, J.,Demo, G.,Komarek, J.,Wimmerova, M. (deposition date: 2018-02-09, release date: 2018-05-16, Last modification date: 2024-05-08) |
| Primary citation | Komarek, J.,Ivanov Kavkova, E.,Houser, J.,Horackova, A.,Zdanska, J.,Demo, G.,Wimmerova, M. Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins. Proteins, 86:897-911, 2018 Cited by PubMed Abstract: 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. PubMed: 29722060DOI: 10.1002/prot.25522 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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