Abstract
3phosphoglycerate dehydrogenase catalyzes the first committed step in serine biosynthesis and the tetrameric enzyme is allosterically inhibited by serine binding to an regulatory domain some 60A from the active site. To investigate the role that ligand induced changes in local motion may play in serine inhibition, local flexibility has been studied using limited proteolysis approaches of both the native protein and a D264N mutation that we have previously shown lacks serine inhibition but binds serine normally. These studies are complemented by an analysis of temperature factors from the crystal structures of native and serine inhibited enzyme and an analysis of the effects of serine on the strength of subunit interactions by dynamic light scattering in the presence and absence of guanidine hydrochloride. Together these approaches shown serine induced changes in local flexibility of the protein rather than simple rotation of rigid domains.This research is supported by a Grant from the National Science Foundation: MCB 0448905 to EB
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