4pfy

Crystal structure of mannohexaose bound oligopeptide ABC transporter, periplasmic oligopeptide-binding protein (TM1223) from THERMOTOGA MARITIMA at 1.5 A resolution

spinqualitylabelsall models 4pfy, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pfy is a 2 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: BMA, MG, NO3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9X0V0_THEMA Publication Abstract from PubMed Many bacteria exist in a state of feast or famine where high nutrient availability leads to periods of growth followed by nutrient scarcity and growth stagnation. To adapt to the constantly changing nutrient flux, metabolite acquisition systems must be able to function over a broad range. This however creates difficulties as nutrient concentrations vary over many orders of magnitude, requiring metabolite acquisition systems to simultaneously balance ligand specificity and the dynamic range in which a response to a metabolite is elicited. Here we present how a gene duplication of a periplasmic binding protein (PBP) in a mannose ABC transport system potentially resolves this dilemma through gene functionalization. Determination of ligand binding affinities and specificities of the gene duplicates with fluorescence and circular dichroism demonstrate that although the binding specificity is maintained the Kd values for the same ligand differ over three orders of magnitude. These results suggest this metabolite acquisition system can transport ligand at both low and high environmental concentrations while preventing saturation with related and less preferentially metabolized compounds. The X-ray crystal structures of the beta mannose bound proteins help clarify the structural basis of gene functionalization and reveal that affinity and specificity are potentially encoded in different regions of the binding site. These studies suggest a possible functional role and adaptive advantage for the presence of two PBPs in ABC transport systems and a way bacteria can adapt to varying nutrient flux through functionalization of gene duplicates. Duplication of genes in an ATP binding cassette transport system increases dynamic range while maintaining ligand specificity.,Ghimire-Rijal S, Lu X, Myles DA, Cuneo MJ J Biol Chem. 2014 Sep 10. pii: jbc.M114.590992. PMID:25210043 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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