A Conformational Switch Underlies ClpP Protease Function

被引：49
作者：
Geiger, Sebastian R. [2 ,3 ]
Boettcher, Thomas [4 ]
Sieber, Stephan A. [1 ]
Cramer, Patrick [2 ,3 ]
机构：
[1] Tech Univ Munich, Dept Chem, Ctr Integrated Prot Sci CIPSM, D-85747 Garching, Germany
[2] Univ Munich, Gene Ctr, D-81377 Munich, Germany
[3] Univ Munich, Dept Biochem, Ctr Integrated Prot Sci CIPSM, D-81377 Munich, Germany
[4] OC II, AVIRU, EXIST Transfer Res, D-85747 Garching, Germany
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2011年 / 50卷 / 25期
关键词：
ClpP heat shock protein; conformational switch; protease complex; protein structures; virulence regulation; PROTEOLYSIS; RECOGNITION;
D O I：
10.1002/anie.201100666
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA"
引用
收藏
页码：5748 / 5751
页数：4
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