We thank Mona Wolff for excellent scientific support and Wolfgang Steglich for helpful discussions. E.Z. was supported by the SFB749 and by the TUM-GS. E.Z. thanks Quan Zhou for helpful discussions. T.B. was supported by the German National Academic Foundation and by an EXIST technology transfer grant of the Federal Ministry of Economics and Technology (BMWi); S.A.S. was supported by the Deutsche Forschungsgemeinschaft (Emmy Noether), SFB749, FOR1406, an ERC starting grant, and the Center for Integrated Protein Science Munich CIPSM. S.W. and N.B. were funded by the DFG (SFB594) and CIPSM.
Communication
Vibralactone as a Tool to Study the Activity and Structure of the ClpP1P2 Complex from Listeria monocytogenes†
Article first published online: 22 SEP 2011
DOI: 10.1002/anie.201104391
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue

Angewandte Chemie International Edition
Volume 50, Issue 46, pages 11001–11004, November 11, 2011
Additional Information
How to Cite
Zeiler, E., Braun, N., Böttcher, T., Kastenmüller, A., Weinkauf, S. and Sieber, S. A. (2011), Vibralactone as a Tool to Study the Activity and Structure of the ClpP1P2 Complex from Listeria monocytogenes. Angew. Chem. Int. Ed., 50: 11001–11004. doi: 10.1002/anie.201104391
- †
Publication History
- Issue published online: 9 NOV 2011
- Article first published online: 22 SEP 2011
- Manuscript Received: 24 JUN 2011
Funded by
- Federal Ministry of Economics and Technology (BMWi)
- Deutsche Forschungsgemeinschaft
- ERC starting grant
- Center for Integrated Protein Science Munich CIPSM
Keywords:
- electron microscopy;
- natural products;
- protein structures;
- proteomics;
- vibralactone

The Clp proteolytic machinery has important functions in many bacteria such as L. monocytogenes. Some organisms encode for two uncharacterized ClpP isoforms. Vibralactone was used to study the activity and assembly of ClpP1 and ClpP2 subunits in a hetero-oligomeric complex. Electron microscopic images reveal that the tetradecameric assembly is made up of two stacked homoheptameric ClpP1 and ClpP2 rings.

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