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Journal Article

A conformational switch underlies ClpP protease function

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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1936187-Suppl-1.mov
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1936187-Suppl-2.pdf
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Citation

Geiger, S. R., Böttcher, T., Sieber, S. A., & Cramer, P. (2011). A conformational switch underlies ClpP protease function. Angewandte Chemie International Edition, 50(25), 5749-5752. doi:10.1002/anie.201100666.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-7D7E-2
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.