Vibralactone as a Tool to Study the Activity and Structure of the ClpP1P2 Complex from <i>Listeria monocytogenes</i>

Abstract

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. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.