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A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF

Title data

Kröger, Pascal ; Shanmugaratnam, Sooruban ; Ferruz, Noelia ; Schweimer, Kristian ; Höcker, Birte:
A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF.
In: Structure. Vol. 29 (6 May 2021) Issue 5 . - pp. 433-443.
ISSN 0969-2126
DOI: https://doi.org/10.1016/j.str.2020.12.005

Abstract in another language

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 1H-15N HSQC NMR spectroscopy. This combined analysis provides a robust framework for understanding ligand binding for future developments in drug design and protein engineering.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Chair Biopolymers - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 11 May 2021 09:03
Last Modified: 11 May 2021 09:03
URI: https://eref.uni-bayreuth.de/id/eprint/65171