This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Sterol methyl transferase (SMT) is an important enzyme that regulates carbon flow in the sterol pathway of fungi. The enzyme catalizes the reaction that transfer a methyl group from (S)-adenosyl-L-methionine to different steriols and other natural products are widespread in biochemstry.New extensive investigations have led to consider a stereochemical model of stearol methylation that describes the topological constraints imposed by sterol substrate in the binding pocket of the SMT. With this regard the crystal structure could represent the experimental fundation of this hyphotetical model and could represent the starting point for the design of new inhibitors of the enzyme. We got the unit cell parameters and a data set with resolution of 5.0 A. Recently we got crystals in different conditions. We need to do X-ray experiments at CHESS to improve the resolution of diffraction data, and to follow with a MAD experiment to solve the phase problem.
Showing the most recent 10 out of 375 publications
