KOMÁREK, Jan, Eva KAVKOVÁ, Josef HOUSER, Aneta HORÁČKOVÁ, Jitka HOLKOVÁ, Gabriel DEMO and Michaela WIMMEROVÁ. Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins. Proteins : structure, function, and genetics. Alan R. Liss, 2018, vol. 86, No 9, p. 897-911. ISSN 0887-3585. Available from: https://dx.doi.org/10.1002/prot.25522. |
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@article{1504096, author = {Komárek, Jan and Kavková, Eva and Houser, Josef and Horáčková, Aneta and Holková, Jitka and Demo, Gabriel and Wimmerová, Michaela}, article_number = {9}, doi = {http://dx.doi.org/10.1002/prot.25522}, keywords = {Agaricus bisporus; bacterial toxins; protein stability; protein structure; toxin-like proteins}, language = {eng}, issn = {0887-3585}, journal = {Proteins : structure, function, and genetics}, title = {Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins}, url = {https://onlinelibrary.wiley.com/doi/full/10.1002/prot.25522}, volume = {86}, year = {2018} }
TY - JOUR ID - 1504096 AU - Komárek, Jan - Kavková, Eva - Houser, Josef - Horáčková, Aneta - Holková, Jitka - Demo, Gabriel - Wimmerová, Michaela PY - 2018 TI - Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins JF - Proteins : structure, function, and genetics VL - 86 IS - 9 SP - 897-911 EP - 897-911 PB - Alan R. Liss SN - 08873585 KW - Agaricus bisporus KW - bacterial toxins KW - protein stability KW - protein structure KW - toxin-like proteins UR - https://onlinelibrary.wiley.com/doi/full/10.1002/prot.25522 L2 - https://onlinelibrary.wiley.com/doi/full/10.1002/prot.25522 N2 - 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. ER -
KOMÁREK, Jan, Eva KAVKOVÁ, Josef HOUSER, Aneta HORÁČKOVÁ, Jitka HOLKOVÁ, Gabriel DEMO and Michaela WIMMEROVÁ. Structure and properties of AB21, a novel Agaricus bisporus protein with structural relation to bacterial pore-forming toxins. \textit{Proteins : structure, function, and genetics}. Alan R. Liss, 2018, vol.~86, No~9, p.~897-911. ISSN~0887-3585. Available from: https://dx.doi.org/10.1002/prot.25522.
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