The first structure-function study of GH151 alpha-l-fucosidase
uncovers new oligomerization pattern, active site
complementation, and selective substrate specificity

J 2022

The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity

KOVALOVA, Terezia, Tomas KOVAL, Jan STRANSKY, Petr KOLENKO, Jarmila DUSKOVA et. al.

Basic information

Original name

The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity

Authors

KOVALOVA, Terezia, Tomas KOVAL, Jan STRANSKY, Petr KOLENKO, Jarmila DUSKOVA, Leona SVECOVA, Patricie VODICKOVA, Vojtech SPIWOK, Eva BENESOVA, Petra LIPOVOVA and Jan DOHNALEK

Edition

FEBS Journal, Hoboken, NJ USA, WILEY-BLACKWELL, 2022, 1742-464X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 5.400

RIV identification code

RIV/00216224:14740/22:00128770

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1111/febs.16387

UT WoS

000757955200001

Keywords in English

active site complementation; crystal structure; GH151; alpha-l-fucosidase

Abstract

V originále

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.

Links

90127, large research infrastructures

Name: CIISB II

Citovat

KOVALOVA, Terezia, Tomas KOVAL, Jan STRANSKY, Petr KOLENKO, Jarmila DUSKOVA, Leona SVECOVA, Patricie VODICKOVA, Vojtech SPIWOK, Eva BENESOVA, Petra LIPOVOVA and Jan DOHNALEK. The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity. FEBS Journal. Hoboken, NJ USA: WILEY-BLACKWELL, 2022, vol. 289, No 16, p. 4998-5020. ISSN 1742-464X. Available from: https://dx.doi.org/10.1111/febs.16387.

@article{2262444,
   author = {Kovalova, Terezia and Koval, Tomas and Stransky, Jan and Kolenko, Petr and Duskova, Jarmila and Svecova, Leona and Vodickova, Patricie and Spiwok, Vojtech and Benesova, Eva and Lipovova, Petra and Dohnalek, Jan},
   article_location = {Hoboken, NJ USA},
   article_number = {16},
   doi = {http://dx.doi.org/10.1111/febs.16387},
   keywords = {active site complementation; crystal structure; GH151; alpha-l-fucosidase},
   language = {eng},
   issn = {1742-464X},
   journal = {FEBS Journal},
   title = {The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity},
   url = {https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16387},
   volume = {289},
   year = {2022}
}

TY  - JOUR
ID  - 2262444
AU  - Kovalova, Terezia - Koval, Tomas - Stransky, Jan - Kolenko, Petr - Duskova, Jarmila - Svecova, Leona - Vodickova, Patricie - Spiwok, Vojtech - Benesova, Eva - Lipovova, Petra - Dohnalek, Jan
PY  - 2022
TI  - The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity
JF  - FEBS Journal
VL  - 289
IS  - 16
SP  - 4998-5020
EP  - 4998-5020
PB  - WILEY-BLACKWELL
SN  - 1742464X
KW  - active site complementation
KW  - crystal structure
KW  - GH151
KW  - alpha-l-fucosidase
UR  - https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16387
N2  - 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.
ER  -

KOVALOVA, Terezia, Tomas KOVAL, Jan STRANSKY, Petr KOLENKO, Jarmila DUSKOVA, Leona SVECOVA, Patricie VODICKOVA, Vojtech SPIWOK, Eva BENESOVA, Petra LIPOVOVA and Jan DOHNALEK. The first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity. \textit{FEBS Journal}. Hoboken, NJ USA: WILEY-BLACKWELL, 2022, vol.~289, No~16, p.~4998-5020. ISSN~1742-464X. Available from: https://dx.doi.org/10.1111/febs.16387.

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