Architecture and Evolution of Blade Assembly in β-propeller Lectins.
carbohydrate binding protein
lectins
oligomerization
β-propeller
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
07 05 2019
07 05 2019
Historique:
received:
04
12
2018
revised:
10
01
2019
accepted:
04
02
2019
pubmed:
12
3
2019
medline:
9
6
2020
entrez:
12
3
2019
Statut:
ppublish
Résumé
Lectins with a β-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 β-propellers using 3D-structural data. With these templates, we predicted 3,887 β-propeller lectins in 1,889 species and organized this information in a searchable online database. The data reveal a widespread distribution of β-propeller lectins across species. Prediction also emphasizes multiple architectures and led to the discovery of a β-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 β-propeller assembly and demonstrates the power of our tools.
Identifiants
pubmed: 30853410
pii: S0969-2126(19)30046-2
doi: 10.1016/j.str.2019.02.002
pii:
doi:
Substances chimiques
Lectins
0
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
764-775.e3Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.