Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Staphylococcus Aureus
SUBMITTER: Barbara Hofbauer
LAB HEAD: Stephan A. Sieber
PROVIDER: PXD015244 | Pride | 2020-05-26
REPOSITORIES: Pride
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Chembiochem : a European journal of chemical biology 20200107 1-2
Caseinolytic protease P (ClpP) is a tetradecameric peptidase that assembles with chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) are small-molecule mimics of ClpX that bind into hydrophobic pockets on the apical site of the complex, thereby activating ClpP. Detection of ClpP has so far been facilitated with active-site-directed probes which depend on the activity and oligomeric state of the complex. To expand the scope of ClpP labeling, we took a stepwise syntheti ...[more]