PXD016304 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Towards the molecular architecture of the peroxisomal receptor docking complex |
Description | Import of yeast peroxisomal matrix proteins is initiated by cytosolic receptors, which specifically recognize and bind the respective cargo proteins. At the peroxisomal membrane, the cargo-loaded receptor interacts with the membrane docking complex, composed of Pex14p, Pex17p and Pex13p. Previous data suggest that this interaction triggers the formation of an import pore for further translocation of the cargo. The mechanistic principles and the underlying mechanism are however unclear, mainly because structures of higher order assemblies are still lacking. Here, using an integrative approach, we provide the first structural characterization of the major components of the peroxisomal docking complex Pex14p/Pex17p, in a native bilayer environment and reveal its subunit organization. Our data show that three copies of Pex14p and a single copy of Pex17p assemble to form a 20 nm rod-like particle. The different subunits are arranged in a parallel manner, showing interactions along their complete sequences and providing receptor binding-sites on both membrane sides. The long rod facing the cytosol is mainly formed by the coiled-coil domains of Pex14p and Pex17p, possibly providing the necessary structural support for the formation of the import pore. Further implications of Pex14p/Pex17p for formation of the peroxisomal translocon are discussed. |
HostingRepository | PRIDE |
AnnounceDate | 2020-12-16 |
AnnouncementXML | Submission_2020-12-16_03:54:09.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Friedel Drepper |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | monohydroxylated residue |
Instrument | Q Exactive; LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-11-18 00:22:13 | ID requested | |
⏵ 1 | 2020-12-16 03:54:09 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: yeast, crosslinking, LC-MS, structural MS, native MS |
Contact List
Bettina Warscheid |
contact affiliation | Functional Proteomics Lab, Faculty of Biology, University of Freiburg, Germany |
contact email | bettina.warscheid@biologie.uni-freiburg.de |
lab head | |
Friedel Drepper |
contact affiliation | AG Warscheid Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany |
contact email | friedel.drepper@biologie.uni-freiburg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD016304
- Label: PRIDE project
- Name: Towards the molecular architecture of the peroxisomal receptor docking complex