6yec

E.coli's Putrescine receptor PotF complexed with Spermine

spinqualitylabelsall models 6yec, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.09Å Ligands: CL, EDO, GOL, PEG, PG4, PGE, SO4, SPM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 (1)H-(15)N HSQC NMR spectroscopy. This combined analysis provides a robust framework for understanding ligand binding for future developments in drug design and protein engineering. A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF.,Kroger P, Shanmugaratnam S, Ferruz N, Schweimer K, Hocker B Structure. 2020 Dec 30. pii: S0969-2126(20)30472-X. doi:, 10.1016/j.str.2020.12.005. PMID:33406388 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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