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.

Základní údaje

Originální název

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

Autoři

KOMÁREK, Jan (203 Česká republika, domácí), Eva KAVKOVÁ (203 Česká republika, domácí), Josef HOUSER (203 Česká republika, domácí), Aneta HORÁČKOVÁ (203 Česká republika, domácí), Jitka HOLKOVÁ (203 Česká republika, domácí), Gabriel DEMO (703 Slovensko, domácí) a Michaela WIMMEROVÁ (203 Česká republika, garant, domácí)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.501

Kód RIV

RIV/00216224:14310/18:00106526

Organizační jednotka

Přírodovědecká fakulta

DOI

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

UT WoS

000446996700001

Klíčová slova anglicky

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

Štítky

CF BIC, CF PROT, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 3. 2019 13:45, prof. RNDr. Michaela Wimmerová, Ph.D.

Anotace

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.

Návaznosti

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

LTC17076, projekt VaV

Název: Interdisciplinární přístup ke studiu biologických systémů na molekulární úrovni

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Interdisciplinární přístup ke studiu biologických systémů na molekulární úrovni, INTER-COST

MUNI/A/1533/2018, interní kód MU

Název: Struktura a dynamika biopolymerů

Investor: Masarykova univerzita, Struktura a dynamika biopolymerů, DO R. 2020_Kategorie A - Specifický výzkum - Studentské výzkumné projekty

Citovat

KOMÁREK, Jan, Eva KAVKOVÁ, Josef HOUSER, Aneta HORÁČKOVÁ, Jitka HOLKOVÁ, Gabriel DEMO a 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, roč. 86, č. 9, s. 897-911. ISSN 0887-3585. Dostupné z: 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 a 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, roč.~86, č.~9, s.~897-911. ISSN~0887-3585. Dostupné z: https://dx.doi.org/10.1002/prot.25522.

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