Structure and mechanism of Escherichia coli type I signal peptidase

Biochimica Et Biophysica Acta
M Paetzel

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.

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Citations

Sep 4, 2014·The Plant Journal : for Cell and Molecular Biology·Takafumi MidorikawaKentaro Inoue
Feb 12, 2015·FEMS Microbiology Reviews·Nienke Buddelmeijer
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Dec 19, 2019·Microbiology and Immunology·Shigeaki MatsudaToshio Kodama
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Feb 18, 2020·Frontiers in Bioengineering and Biotechnology·Alexandros KaryolaimosJan-Willem de Gier
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