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Conformational control of the bacterial Clp protease by natural product antibiotics

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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

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Publication details

The article was received on 24 Dec 2016 and first published on 04 Apr 2017


Article type: Review Article
DOI: 10.1039/C6NP00125D
Citation: Nat. Prod. Rep., 2017, Advance Article
  • Open access: Creative Commons BY-NC license
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    Conformational control of the bacterial Clp protease by natural product antibiotics

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

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