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

J 2018

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

KOMÁREK, Jan, Eva KAVKOVÁ, Josef HOUSER, Aneta HORÁČKOVÁ, Jitka HOLKOVÁ et. al.

Basic information

Original name

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

Authors

KOMÁREK, Jan (203 Czech Republic, belonging to the institution), Eva KAVKOVÁ (203 Czech Republic, belonging to the institution), Josef HOUSER (203 Czech Republic, belonging to the institution), Aneta HORÁČKOVÁ (203 Czech Republic, belonging to the institution), Jitka HOLKOVÁ (203 Czech Republic, belonging to the institution), Gabriel DEMO (703 Slovakia, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Proteins : structure, function, and genetics, Alan R. Liss, 2018, 0887-3585

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 2.501

RIV identification code

RIV/00216224:14310/18:00106526

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1002/prot.25522

UT WoS

000446996700001

Keywords in English

Agaricus bisporus; bacterial toxins; protein stability; protein structure; toxin-like proteins

Abstract

V originále

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.

Links

LM2015043, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

LTC17076, research and development project

Name: Interdisciplinární přístup ke studiu biologických systémů na molekulární úrovni

Investor: Ministry of Education, Youth and Sports of the CR, Interdisciplinary approach to study biological systems at the molecular level, INTER-COST

MUNI/A/1533/2018, interní kód MU

Name: Struktura a dynamika biopolymerů

Investor: Masaryk University, Category A

Citovat

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.

@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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