Jump to main content
Jump to site search

Issue 7, 2017
Previous Article Next Article

Conformational control of the bacterial Clp protease by natural product antibiotics

Author affiliations

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

Back to tab navigation

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., 2017,34, 815-831
  • Open access: Creative Commons BY-NC license
  •   Request permissions

    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

    This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements