A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF.
X-ray crystallography
biogenic amines
isothermal titration calorimetry
molecular dynamics simulation
nuclear magnetic resonance spectroscopy
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
06 05 2021
06 05 2021
Historique:
received:
07
08
2020
revised:
28
10
2020
accepted:
08
12
2020
pubmed:
7
1
2021
medline:
30
11
2021
entrez:
6
1
2021
Statut:
ppublish
Résumé
Periplasmic binding proteins (PBPs) are ubiquitous receptors in gram-negative bacteria. They sense solutes and play key roles in nutrient uptake. Escherichia coli's putrescine receptor PotF has been reported to bind putrescine and spermidine. We reveal that several similar biogenic polyamines are recognized by PotF. Using isothermal titration calorimetry paired with X-ray crystallography of the different complexes, we unveil PotF's binding modes in detail. The binding site for PBPs is located between two lobes that undergo a large conformational change upon ligand recognition. Hence, analyzing the influence of ligands on complex formation is crucial. Therefore, we solved crystal structures of an open and closed apo state and used them as a basis for molecular dynamics simulations. In addition, we accessed structural behavior in solution for all complexes by
Identifiants
pubmed: 33406388
pii: S0969-2126(20)30472-X
doi: 10.1016/j.str.2020.12.005
pii:
doi:
Substances chimiques
Escherichia coli Proteins
0
Ligands
0
Periplasmic Binding Proteins
0
Polyamines
0
Receptors, Biogenic Amine
0
potF protein, E coli
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
433-443.e4Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.