A conformational switch underlies ClpP protease function

Sebastian R. Geiger; Thomas Böttcher; Stephan A. Sieber; Patrick Cramer

doi:10.1002/anie.201100666

A conformational switch underlies ClpP protease function

Sebastian R. Geiger, Thomas Böttcher, Stephan A. Sieber, Patrick Cramer

Chair of Organic Chemistry II

Research output: Contribution to journal › Article › peer-review

55 Scopus citations

Abstract

A "breathing" protein: The first structure of the virulence regulator and heat shock protein ClpP from Staphylococcus aureus reveals a previously unobserved compressed state of the ClpP barrel. A conformational switch in the active center "handle region" results in closure of the active sites and opening of equatorial pores. These results confirm proposed modes of processive substrate degradation and product release for the ClpP protease family.

Original language	English
Pages (from-to)	5749-5752
Number of pages	4
Journal	Angewandte Chemie International Edition in English
Volume	50
Issue number	25
DOIs	https://doi.org/10.1002/anie.201100666
State	Published - 14 Jun 2011

Keywords

ClpP heat shock protein
conformational switch
protease complex
protein structures
virulence regulation

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10.1002/anie.201100666

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AU - Böttcher, Thomas

AU - Sieber, Stephan A.

AU - Cramer, Patrick

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KW - ClpP heat shock protein

KW - conformational switch

KW - protease complex

KW - protein structures

KW - virulence regulation

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A conformational switch underlies ClpP protease function

Abstract

Keywords

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