| 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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