Structural Basis of Glycerophosphodiester Recognition by the <i>Mycobacterium tuberculosis</i> Substrate-Binding Protein UgpB.

ABSTRACT: 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

SUBMITTER: Fenn JS 

PROVIDER: S-EPMC6757277 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature