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[1].
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). [2].
3D structures of glucose-1-phosphate thymidylyltransferase
Glucose-1-phosphate thymidylyltransferase 3D structures
