Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors

Author:

Felix Jan1ORCID,Weinhäupl Katharina1,Chipot Christophe234ORCID,Dehez François23ORCID,Hessel Audrey1,Gauto Diego F.1,Morlot Cecile1,Abian Olga5678,Gutsche Irina1ORCID,Velazquez-Campoy Adrian5679,Schanda Paul1ORCID,Fraga Hugo11011ORCID

Affiliation:

1. Institut de Biologie Structurale, Université Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des Martyrs, F-38044 Grenoble, France.

2. LPCT, UMR 7019 Université de Lorraine CNRS, Vandoeuvre-les-Nancy F-54500, France.

3. Laboratoire International Associé CNRS and University of Illinois at Urbana−Champaign, Vandoeuvre-les-Nancy F-54506, France.

4. Department of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street, Urbana, IL 61801, USA.

5. Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Units IQFR-CSIC-BIFI and GBsC-CSIC-BIFI, and Department of Biochemistry and Molecular and Cell Biology, Universidad de Zaragoza, 50018 Zaragoza, Spain.

6. Aragon Institute for Health Research (IIS Aragon), 50009 Zaragoza, Spain.

7. Biomedical Research Networking Centre for Liver and Digestive Diseases (CIBERehd), Madrid, Spain.

8. Aragon Health Sciences Institute (IACS), 50009 Zaragoza, Spain.

9. Fundacion ARAID, Government of Aragon, 50018 Zaragoza, Spain.

10. Departamento de Biomedicina, Faculdade de Medicina da Universidade do Porto, Porto, Portugal.

11. i3S, Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.

Abstract

We decipher how an allosteric inhibitor activates the ClpP protease machinery by binding to the catalytic site.

Funder

FP7 Ideas: European Research Council

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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