Structurally Sound — In the June 4 issue of Structure, Drs. Vern Schramm, Steven Almo and Antti Haapalainen report their use of crystallography – a method used to determine molecular structures by examining them in crystalline form – to identify novel inhibitors of a key enzyme of the bacteria Salmonella enterica. This enzyme, called MTAN (MTA/SAH nucleosidase), is responsible for metabolism of the amino acid methionine and is only expressed by bacteria, making it an ideal target for developing antibiotics. Drs. Schramm and Almo analyzed the crystal structure of MTAN and used this structural information to develop rational design of inhibitors that bind to the enzyme very strongly, identifying new possible antibiotics against S. enterica as well as a method that can be used to develop inhibitors of other bacterial targets. Dr. Schramm is professor and chair of biochemistry and the Ruth Merns Chair in Biochemistry; Dr. Almo is professor of biochemistry and holds the Wollowick Family Foundation Chair in Multiple Sclerosis and Immunology; Dr. Haapalainen is a postdoctoral fellow in the Schramm lab.
Posted on: Monday, July 08, 2013