This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Three-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase catalyses a committed step in the pathways for isoprenoid, cholesterol, and ketone body production. Recently, the structure of bacterial HMG-CoA synthase was published. Our work is focused on a eukaryote HMG-CoA synthase. Crystals were screened using the in-house x-ray source, they showed a good diffraction, but the spots were too close to be able to process the data. However, the structure could be solved at the ESRF synchrotron by taking images every 0.25 , the processing revealed a huge unit cell (61x61x412). Our current first priority is to get the structure of inhibitors bound in the active site. Crystals of wild-type, as well as mutant, enzyme-inhibitors complexes have been obtained. The huge unit cell edge forces the use of synchrotron radiation.
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