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- W2000301649 abstract "The phosphoenolpyruvate-dependent phosphotranferase system (PTS) is responsible for the uni-directional, phosphorylation-coupled uptake of sugar in bacteria. The multicomponent PTS differs from other carbohydrate uptake systems in that active transport is driven by coupling the translocation of the ligand across the membrane with its concomitant covalent modification to prevent efflux. Crystal structures have been solved previously for the numerous cytoplasmic proteins involved in the PTS pathway, but a complete understanding of the system has until now been hampered by the lack of any structures for the integral membrane component EIIC. The EIICs are a large, diverse family of carbohydrate transporters that selectively bind a cognate sugar, translocate it across the inner membrane, and assist in the phosphorylation reaction. In order to better understand how these functions are carried out, we have solved the 3.3 A structure of an ortholog of the transporter ChbC. This member of the glucose EIIC superfamily is specific for the uptake of N.N’-diacetylchitobiose, a component of chitin and important food source in a number of pathogens. The structure shows that ChbC possesses a novel fold, and has led us to propose a mechanism for how the transporter couples phosphorylation and transport of its substrate. We are now attempting a variety of functional assays to characterize the sugar selectivity of the transporter, as well as to elucidate the mechanism of phosphorylation and transport." @default.
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- W2000301649 date "2011-02-01" @default.
- W2000301649 modified "2023-09-25" @default.
- W2000301649 title "Mechanism of Sugar Transport by a Phosphoenolpyruvate-Dependent Phosphotransferase" @default.
- W2000301649 doi "https://doi.org/10.1016/j.bpj.2010.12.2166" @default.
- W2000301649 hasPublicationYear "2011" @default.
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