A conformational switch underlies ClpP protease function

Geiger, S. R.; Böttcher, T.; Sieber, S. A.; Cramer, P.

doi:10.1002/anie.201100666

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

A conformational switch underlies ClpP protease function

MPS-Authors

/persons/resource/persons127020

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

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

1936187-Suppl-1.mov
(Supplementary material), 4MB

1936187-Suppl-2.pdf
(Supplementary material), 206KB

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: https://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.