Počet záznamů: 1
The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity
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SYSNO ASEP 0560263 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity Tvůrce(i) Koval'ová, Terezia (BTO-N)
Koval, Tomáš (BTO-N) ORCID
Stránský, Jan (BTO-N) RID
Kolenko, Petr (BTO-N) ORCID, RID
Dušková, Jarmila (BTO-N) RID, SAI
Švecová, Leona (BTO-N)
Vodickova, P. (CZ)
Spiwok, V. (CZ)
Benešová, E. (CZ)
Lipovová, P. (CZ)
Dohnálek, Jan (BTO-N) RID, ORCIDCelkový počet autorů 11 Číslo článku 16387 Zdroj.dok. FEBS Journal - ISSN 1742-464X
Roč. 289, č. 16 (2022)Poč.str. 23 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova active site complementation ; crystal structure ; gh151 ; alpha-l-fucosidase Vědní obor RIV EB - Genetika a molekulární biologie Obor OECD Biochemistry and molecular biology CEP LM2015043 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy EF15_003/0000447 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy EF16_013/0001776 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy ED1.1.00/02.0109 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LM2018127 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Omezený přístup Institucionální podpora BTO-N - RVO:86652036 UT WOS 000757955200001 EID SCOPUS 85124872855 DOI 10.1111/febs.16387 Anotace Fucosylated compounds are abundantly present in nature and are associated with many biological processes, therefore carrying great potential for use in medicine and biotechnology. Efficient ways to modify fucosylated compounds are still being developed. Promising results are provided by glycosyl hydrolases with transglycosylating activities, such as alpha-l-fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus (family GH151 of Carbohydrate-Active enZYmes). Currently, there is no 3D structure representing this glycoside hydrolase family and only a few members have been investigated. Here, we present the first structure-function study of a GH151 member, providing the key insights into its specific oligomerization and active site properties. According to the crystal structure, small-angle X-ray scattering data and catalytic investigation, this enzyme functions as a tetramer of a new type and represents the second known case of active site complementation among all alpha-l-fucosidases. Mutation of the active site-complementing residue histidine 503 to alanine confirmed its influence on alpha-l-fucosidase activity and, specifically, on substrate binding. Several unique features of GH151 family alpha-l-fucosidases were revealed, including the oligomerization pattern, active site accessibility and complementation, and substrate selectivity. Some common properties of GH151 glycosyl hydrolases then would be the overall three-domain structure and conservation of the central domain loop 2 function, including its complementation role and the formation of the carbohydrate-binding platform in the active site vicinity. Pracoviště Biotechnologický ústav Kontakt Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Rok sběru 2023 Elektronická adresa https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16387
Počet záznamů: 1