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
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.e4

Informations de copyright

Copyright © 2020 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

Auteurs

Pascal Kröger (P)

Department of Biochemistry, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany.

Sooruban Shanmugaratnam (S)

Department of Biochemistry, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany.

Noelia Ferruz (N)

Department of Biochemistry, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany.

Kristian Schweimer (K)

Department of Biochemistry, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany; Northern Bavarian NMR Center, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany.

Birte Höcker (B)

Department of Biochemistry, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany. Electronic address: birte.hoecker@uni-bayreuth.de.

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Classifications MeSH