Carbohydrate-Binding Capability and Functional Conformational Changes of AbnE, an Arabino-oligosaccharide Binding Protein.
ABC transporter
Arabinan utilization system
Geobacillus stearothermophilus
arabinose
substrate-binding protein
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
27 03 2020
27 03 2020
Historique:
received:
10
10
2019
revised:
19
01
2020
accepted:
30
01
2020
pubmed:
19
2
2020
medline:
28
8
2020
entrez:
19
2
2020
Statut:
ppublish
Résumé
ABC importers are membrane proteins responsible for the transport of nutrients into the cells of prokaryotes. Although the structures of ABC importers vary, all contain four conserved domains: two nucleotide-binding domains (NBDs), which bind and hydrolyze ATP, and two transmembrane domains (TMDs), which help translocate the substrate. ABC importers are also dependent on an additional protein component, a high-affinity substrate-binding protein (SBP) that specifically binds the target ligand for delivery to the appropriate ABC transporter. AbnE is a SBP belonging to the ABC importer for arabino-oligosaccharides in the Gram-positive thermophilic bacterium Geobacillus stearothermophilus. Using isothermal titration calorimetry (ITC), purified AbnE was shown to bind medium-sized arabino-oligosaccharides, in the range of arabino-triose (A3) to arabino-octaose (A8), all with K
Identifiants
pubmed: 32067952
pii: S0022-2836(20)30107-8
doi: 10.1016/j.jmb.2020.01.041
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Arabinose
B40ROO395Z
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2099-2120Informations de copyright
Copyright © 2020. Published by Elsevier Ltd.