The structure of dienelactone hydrolase (DLH) has been solved and is currently being refined at high resolution. Dr. Ollis plans to determine the enzymatic mechanism of DLH using a combination of solution studies and substrate binding studies with the crystalline protein. He will also structurally and chemically characterize the catalytic triad of DLH using both diffraction methods and NMR. In addition, crystals of two proteins that interact with DNA, a single stranded binding protein and a DNA ligase, have been obtained and will now be studied. The study of how organisms evolve to utilize new nutrient sources is both fascinating and of critical importance for the survival of living systems. The enzyme DLH is an ideal model system to understand this evolution at a molecular level. DLH is a component of the ketoadipate pathway which operates in bacteria and fungi and which possesses of a number of different branches, in each of which catechol or a catechol derivative is catabolized.
