PXD015244 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Acyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state |
Description | Caseinolytic protease P (ClpP) is a tetradecameric peptidase which assembles with chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) represent small molecule mimics of ClpX, which bind into hydrophobic pockets on the apical site of the complex and thereby induce activation of 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. In order to expand the scope of ClpP labeling, we here introduce a stepwise synthetic approach to customized ADEP photoprobes. Structure-activity relationship studies with small fragments and ADEP derivatives paired with modeling studies revealed design principles of suitable probe molecules. The derivatives were tested for activation of ClpP and subsequently applied in labeling studies of the wild type peptidase as well as enzymes bearing mutations at the active site and an oligomerization sensor. Satisfyingly, the ADEP photoprobes provided a labeling readout of ClpP independent of its activity and oligomeric state. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_05:05:21.692.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Barbara Hofbauer |
SpeciesList | scientific name: Staphylococcus aureus; NCBI TaxID: 1280; |
ModificationList | monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-08-30 03:55:30 | ID requested | |
1 | 2020-05-26 14:31:17 | announced | |
⏵ 2 | 2024-10-22 05:05:22 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1002/cbic.201900477; |
Eyermann B, Meixner M, Br, ö, tz-Oesterhelt H, Antes I, Sieber SA, P Independent of Its Oligomeric and Activity State. Chembiochem, 21(1-2):235-240(2020) [pubmed] |
Keyword List
curator keyword: Biological, Biomedical |
submitter keyword: Thermo Fischer Q Exactive Orbitrap,photoaffinity labeling, S. aureus |
Contact List
Stephan A. Sieber |
contact affiliation | Department of Chemistry Chair of Organic Chemistry II Technical University of Munich Germany |
contact email | stephan.sieber@tum.de |
lab head | |
Barbara Hofbauer |
contact affiliation | Technische Universität München |
contact email | b.hofbauer@tum.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD015244
- Label: PRIDE project
- Name: Acyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state