6wce

Structure of the periplasmic binding protein P5PA

spinqualitylabelsall models 6wce, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6wce is a 1 chain structure with sequence from Actinobacillus pleuropneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.754Å Ligands: PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B0BUC2_ACTPJ Publication Abstract from PubMed Bacteria require high efficiency uptake systems to survive and proliferate in nutrient limiting environments, such as those found in host organisms. ATP binding cassette (ABC) transporters in the bacterial plasma membrane provide a mechanism for transport of many substrates. In this study, we examine an operon containing a periplasmic binding protein in Actinobacillus for its potential role in nutrient acquisition. The 1.76 A resolution electron density map obtained from the crystal structure of the periplasmic binding protein was best fit with a molecular model containing a pyridoxal-5'-phosphate (P5P/PLP/the active form of vitamin B6) ligand within the protein's binding site. The identity of the P5P bound to this periplasmic binding protein was verified by isothermal titration calorimetry, microscale thermophoresis, and mass spectrometry, leading us to name the protein P5PA and the operon P5PAB. To illustrate the functional utility of this uptake system, we introduced the P5PAB operon from A. pleuropneumoniae into an E. coli K-12 strain that was devoid of a key enzyme required for P5P synthesis. The growth of this strain at low levels of P5P supports the functional role of this operon in P5P uptake. This is the first report of a dedicated P5P bacterial uptake system, but through bioinformatics we discovered homologs mainly within pathogenic representatives of the Pasteurellaceae family, suggesting that this operon exists more widely outside the Actinobacillus genus. Actinobacillus utilizes a binding-protein dependent ABC transporter to acquire the active form of Vitamin B6.,Pan C, Zimmer A, Shah M, Huynh MS, Chieh-Lin Lai C, Sit B, Hooda Y, Curran DM, Moraes TF J Biol Chem. 2021 Aug 3:101046. doi: 10.1016/j.jbc.2021.101046. PMID:34358566 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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