Glucose-1-phosphate thymidylyltransferase

Function Glucose-1-phosphate thymidylyltransferase (RmlA) catalyzes the conversion of dTTP and α-D-glucose 1-phosphate (DGP) to diphosphate and dTDP-glucose or dTDP- rhamnose. RmlA participates in nucleotide sugars metabolism, streptomycin biosynthesis and polyketide sugar metabolism. Relevance dTDP- rhamnose is a component of bacterial cell wall, hence RmlA inhibition is a potential therapeutic target as drugs against pathogenic bacteria. Structural highlights RmlA 3D structure can be divided into three functional domains: a core domain which binds . The is formed by the core and sugar-binding domains and the residues comprising it can be divided to catalytic residues (in cyan) and thymidine-specific residues (in green). . 3D structures of glucose-1-phosphate thymidylyltransferase Glucose-1-phosphate thymidylyltransferase 3D structures

spinqualitylabelsall models Structure of glucose-1-phosphate thymidylyltransferase complex with TTP (PDB code 1g2v). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image