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

University of Munich
Lawrence Berkeley National Laboratory
Aviru Exist

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

61 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
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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keywords = "ClpP heat shock protein, conformational switch, protease complex, protein structures, virulence regulation",

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AU - Geiger, Sebastian R.

AU - Böttcher, Thomas

AU - Sieber, Stephan A.

AU - Cramer, Patrick

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Y1 - 2011/6/14

N2 - 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.

AB - 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.

KW - ClpP heat shock protein

KW - conformational switch

KW - protease complex

KW - protein structures

KW - virulence regulation

UR - https://www.scopus.com/pages/publications/79958250888

U2 - 10.1002/anie.201100666

DO - 10.1002/anie.201100666

M3 - Article

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AN - SCOPUS:79958250888

SN - 1433-7851

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 25

ER -

A conformational switch underlies ClpP protease function

Abstract

Keywords

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