Research description Our laboratory studies the three-dimensional structures of proteins relevant to human disease. A major focus of the lab is characterizing proteins in an enzyme superfamily known as the alpha-D-phosphohexomutases. These enzymes catalyze the production of phosphorylated sugar precursors that are assembled into more complex carbohydrates, such as polysaccharides. Enzymes in this superfamily are found in all organisms, including bacteria, archaea, and eukaryotes. In many bacteria, polysaccharides are critical determinants of infectivity, and so these enzymes are excellent targets for the design of antimicrobial agents. In humans, deficiency in the enzyme phosphoglucomutase 1 (PGM1) has been recently identified as an inherited metabolic disease categorized as both a muscle glycogenosis (type XIV) and a congenital disorder of glycosylation (CDG types I and II).