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首页> 外文期刊>Biochimica et biophysica acta. Molecular cell research >Structure and mechanism of Escherichia coli type I signal peptidase
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Structure and mechanism of Escherichia coli type I signal peptidase

机译:大肠杆菌I型信号肽酶的结构和机制

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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.
机译:I型信号肽酶是负责从细菌细胞质膜上分泌的蛋白质中切割出氨基末端信号肽的酶。它是一种必不可少的膜结合酶,其丝氨酸/赖氨酸催化二聚体位于细菌膜的胞外表面。这篇综述讨论了在大肠杆菌I型信号肽酶(SPase I)的结构和机理表征方面取得的进展,以及基于SPase I抑制作用开发新型抗生素的努力。本文是名为“蛋白质在细菌中的运输和分泌”的特刊的一部分。客座编辑:Anastassios Economou和Ross Dalbey。

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