Structural basis for dimerization and catalysis of a novel sterase from the GTSAG motif subfamily of the bacterial hormone-sensitive lipase family

Abstract

Background: Catalytic mechanisms of GTSAG motif subfamily enzymes of the bacterial hormone-sensitive lipases (HSLs) family are largely unknown. Results: E25, a GTSAG motif subfamily esterase, adopts a novel dimerization pattern. Dimerization keeps the catalytic Asp282 orientation for E25 catalysis. Conclusion: Dimerization and some catalytic profiles of E25 are distinctive from other HSLs. Significance: Our study sheds light on protein folding and evolution of HSLs. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.