Large scale structural rearrangement of a serine hydrolase from francisella tularensis facilitates catalysis

Abstract

Background: Acyl protein thioesterases control protein S-acylation at cellular membranes. Results: FTT258 is a serine hydrolase with broad substrate specificity that binds to bacterial membranes and exists in two distinct conformations. Conclusion: Conformational changes in FTT258 are correlated with catalytic activity. Significance: Structural rearrangement dually regulates the membrane binding and catalytic activity of acyl protein thioesterases. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.