PROBING THE LIGAND INDUCED CONFORMATIONAL CHANGE OF BETA-PHOSPHOGLUCOMUTASE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The proposed experiments aim to identify the major protein-ligand interactions that induce the conformational change previously observed by X-ray crystallography in beta-phosphoglucomutase (bPGM). bPGM is part of the largest subfamily of the ubiquitous Haloalkanoate Dehalogenase Superfamily (HADSF) that performs the bulk of phosphoryl transfer in nature. Identification of the crucial ligand-protein interactions responsible for the conformational change will give insight into the mechanism of this transition and the evolution of substrate specificity in this subfamily. These studies will also provide a useful model system for the study of protein-ligand interactions via SAXS. Rapid access is requested to allow for initial data collection towards a full proposal as well as to provide preliminary results for funding opportunities in this area.