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A Conformational Switch Underlies ClpP Protease Function
Author(s) -
Geiger Sebastian R.,
Böttcher Thomas,
Sieber Stephan A.,
Cramer Patrick
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201100666
Subject(s) - protease , biophysics , structure function , virulence , regulator , chemistry , substrate (aquarium) , microbiology and biotechnology , active site , barrel (horology) , enzyme , biology , biochemistry , materials science , physics , ecology , particle physics , gene , composite material
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.