6r1b

Crystal structure of UgpB from Mycobacterium tuberculosis in complex with glycerophosphocholine

spinqualitylabelsall models 6r1b, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r1b is a 4 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2700021Å Ligands: CH5, GOL, MG, MLZ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P71619_MYCTU Publication Abstract from PubMed Mycobacterium tuberculosis (Mtb) is the causative agent of tuberculosis (TB) and has evolved an incredible ability to survive latently within the human host for decades. The Mtb pathogen encodes for a low number of ATP-binding cassette (ABC) importers for the acquisition of carbohydrates that may reflect the nutrient poor environment within the host macrophages. Mtb UgpB (Rv2833c) is the substrate binding domain of the UgpABCE transporter that recognizes glycerophosphocholine (GPC), indicating that this transporter has a role in recycling glycerophospholipid metabolites. By using a combination of saturation transfer difference (STD) NMR and X-ray crystallography, we report the structural analysis of Mtb UgpB complexed with GPC and have identified that Mtb UgpB not only recognizes GPC but is also promiscuous for a broad range of glycerophosphodiesters. Complementary biochemical analyses and site-directed mutagenesis precisely define the molecular basis and specificity of glycerophosphodiester recognition. Our results provide critical insights into the structural and functional role of the Mtb UgpB transporter and reveal that the specificity of this ABC-transporter is not limited to GPC, therefore optimizing the ability of Mtb to scavenge scarce nutrients and essential glycerophospholipid metabolites via a single transporter during intracellular infection. Structural Basis of Glycerophosphodiester Recognition by the Mycobacterium tuberculosis Substrate-Binding Protein UgpB.,Fenn JS, Nepravishta R, Guy CS, Harrison J, Angulo J, Cameron AD, Fullam E ACS Chem Biol. 2019 Sep 20;14(9):1879-1887. doi: 10.1021/acschembio.9b00204. Epub , 2019 Aug 21. PMID:31433162 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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