6mlj | pdb_00006mlj

Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) S70A mutant from Salmonella typhimurium complexed with arginine

spinqualitylabelsall models 6mlj, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mlj is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: ACT, ARG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ARGT_SALTY This periplasmic binding protein is involved in an arginine transport system. ArgT and histidine-binding protein J (HisJ) interact with a common membrane-bound receptor, HisP. Publication Abstract from PubMed The study of binding thermodynamics is essential to understand how affinity and selectivity are acquired in molecular complexes. Periplasmic binding proteins (PBPs) are macromolecules of biotechnological interest that bind a broad number of ligands and have been used to design biosensors. The lysine-arginine-ornithine binding protein (LAO) is a PBP of 238 residues that binds the basic amino acids l-arginine and l-histidine with nm and mum affinity, respectively. It has been shown that the affinity difference for arginine and histidine binding is caused by enthalpy, this correlates with the higher number of protein-ligand contacts formed with arginine. In order to elucidate the structural bases that determine binding affinity and selectivity in LAO, the contribution of protein-ligand contacts to binding energetics was assessed. To this end, an alanine scanning of the LAO-binding site residues was performed and arginine and histidine binding were characterized by isothermal titration calorimetry and X-ray crystallography. Although unexpected enthalpy and entropy changes were observed in some mutants, thermodynamic data correlated with structural information, especially, the binding heat capacity change. We found that selectivity is conferred by several residues rather than exclusive arginine-protein interactions. Furthermore, crystallographic structures revealed that protein-ligand contributions to binding thermodynamics are highly influenced by the solvent. Finally, we found a similar backbone conformation in all the closed structures obtained, but different structures in the open state, suggesting that the binding site residues of LAO play an important role in stabilizing not only the holo conformation, but also the apo state. DATABASE: Structural data are available in the Protein Data Bank database under the accession numbers 6MLE, 6MLN, 6MLG, 6MKX, 6MLI, 6MLA, 6MKU, 6MKW, 6ML0, 6MLD, 6MLV, 6MLO, 6MLP, 6ML9, 6MLJ. The interplay of protein-ligand and water-mediated interactions shape affinity and selectivity in the LAO binding protein.,Vergara R, Romero-Romero S, Velazquez-Lopez I, Espinoza-Perez G, Rodriguez-Hernandez A, Pulido NO, Sosa-Peinado A, Rodriguez-Romero A, Fernandez-Velasco DA FEBS J. 2019 Jul 26. doi: 10.1111/febs.15019. PMID:31348608 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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