Detailed Information on Publication Record
2019
Architecture and Evolution of Blade Assembly in beta-propeller Lectins
BONNARDEL, Francois, Atul KUMAR, Michaela WIMMEROVÁ, Martina LAHMANN, Serge PEREZ et. al.Basic information
Original name
Architecture and Evolution of Blade Assembly in beta-propeller Lectins
Authors
BONNARDEL, Francois (250 France), Atul KUMAR (356 India, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution), Martina LAHMANN (752 Sweden), Serge PEREZ (250 France), Annabelle VARROT (250 France), Frederique LISACEK (756 Switzerland) and Anne IMBERTY (250 France)
Edition
Structure, CAMBRIDGE, CELL PRESS, 2019, 0969-2126
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10400 1.4 Chemical sciences
Country of publisher
Switzerland
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.862
RIV identification code
RIV/00216224:14310/19:00108109
Organization unit
Faculty of Science
UT WoS
000467238900006
Keywords in English
lectin; beta-propellers
Tags
International impact, Reviewed
Změněno: 27/10/2024 14:59, Ing. Martina Blahová
Abstract
V originále
Lectins with a beta-propeller fold bind glycans on the cell surface through multivalent binding sites and appropriate directionality. These proteins are formed by repeats of short domains, raising questions about evolutionary duplication. However, these repeats are difficult to detect in translated genomes and seldom correctly annotated in sequence databases. To address these issues, we defined the blade signature of the five types of beta-propellers using 3D-structural data. With these templates, we predicted 3,887 beta-propeller lectins in 1,889 species and organized this information in a searchable online database. The data reveal a widespread distribution of beta-propeller lectins across species. Prediction also emphasizes multiple architectures and led to the discovery of a beta-propeller assembly scenario. This was confirmed by producing and characterizing a predicted protein coded in the genome of Kordia zhangzhouensis. The crystal structure uncovers an intermediate in the evolution of beta-propeller assembly and demonstrates the power of our tools.
Links
GA18-18964S, research and development project |
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LQ1601, research and development project |
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692068, interní kód MU |
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90043, large research infrastructures |
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