Issue 7, 2017

Conformational control of the bacterial Clp protease by natural product antibiotics

Abstract

Covering: up to 2017

The bacterial Clp protease is a highly conserved and structurally versatile machine. It has gained a lot of recognition during the last decade as a novel antibacterial drug target with an unprecedented mechanism of action. Due to its complexity, there are distinct means of interfering with its natural functions and several compounds targeting this machine have been identified. In this review, we summarize the current state of knowledge about natural products deregulating Clp proteolysis, a crucial and delicate process within the cell. Among those, acyldepsipeptide antibiotics of the ADEP class (ADEPs) are characterized best. The molecular mechanism of ADEP-mediated deregulation sheds light on the inner workings of the Clp protease.

Graphical abstract: Conformational control of the bacterial Clp protease by natural product antibiotics

Article information

Article type
Review Article
Submitted
24 Dec. 2016
First published
04 Apr. 2017
This article is Open Access
Creative Commons BY-NC license

Nat. Prod. Rep., 2017,34, 815-831

Conformational control of the bacterial Clp protease by natural product antibiotics

I. T. Malik and H. Brötz-Oesterhelt, Nat. Prod. Rep., 2017, 34, 815 DOI: 10.1039/C6NP00125D

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