Catalytic Action of Proteins:
A system we are examining involves a unique hexameric form of the enzyme citrate synthase, which is only found in Gram-negative bacteria. This key metabolic enzyme is allosterically controlled by an unknown mechanism. Our lab has recently solved the complete three-dimensional structure of the enzyme and begun the process of unraveling the structure-function relationships that control its catalytic activity. Given the central role this enzyme plays in the metabolism of Gram-negative pathogens, understanding its mechanism of action could potentially allow for the development of novel anti-microbial compounds.
Relevant NGDI Articles
Enzyme-substrate complexes of allosteric citrate synthase: Evidence for a novel intermediate in substrate binding. Duckworth HW, Nguyen NT, Gao Y, Donald LJ, Maurus R, Ayed A, Bruneau B, Brayer GD. Biochim Biophys Acta. 2013 Dec;1834(12):2546-53.
The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode. Caner S, Nguyen N, Aguda A, Zhang R, Pan YT, Withers SG, Brayer GD. Glycobiology. 2013 Sep;23(9):1075-83.