title: Structure and mechanism of Escherichia coli type I signal peptidase.
abstract: Type I signal peptidase is the enzyme responsible for cleaving off the amino-terminal signal peptide from proteins that are secreted across the bacterial cytoplasmic membrane. It is an essential membrane bound enzyme whose serine/lysine catalytic dyad resides on the exo-cytoplasmic surface of the bacterial membrane. This review discusses the progress that has been made in the structural and mechanistic characterization of Escherichia coli type I signal peptidase (SPase I) as well as efforts to develop a novel class of antibiotics based on SPase I inhibition. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.
authors: Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, British Columbia V5A 1S6, Canada. Electronic address: mpaetzel@sfu.ca.
authors: Mark
authors: M
authors: Paetzel
mesh_terms: D001665:Binding Sites; D002462:Cell Membrane / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D021382:Protein Sorting Signals; D021381:Protein Transport / Q000235:genetics; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D021382:Protein Sorting Signals; D012697:Serine Endopeptidases; C026515:type I signal peptidase
keywords: Leader peptidase; Leader peptide; Preprotein processing; Protein secretion; Signal peptidase; Signal peptide