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PXD054394

PXD054394 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleInterdomain-linker control conformational transitions in the SLC23 elevator transporter UraA
DescriptionUptake of nucleobases and ascorbate is an essential process in all living organisms mediated by SLC23 transport proteins. These transmembrane carriers operate via the elevator alternating access mechanism and are composed of two rigid domains whose relative motion drives transport. The lack of large conformational changes within these domains suggests that the interdomain-linkers act as flexible tethers. Here, we show that interdomain-linkers are not mere tethers but have a key regulatory role in dictating the conformational space of the transporter and defining the rotation axis of the mobile transport domain. By resolving a wide inward-open conformation of the SLC23 elevator transporter UraA and combining biochemical studies using a synthetic nanobody as conformational probe with hydrogen-deuterium exchange mass spectrometry, we demonstrate that interdomain-linkers control the function of transport proteins by influencing substrate affinity and transport rate. These findings open the possibility to allosterically modulate the activity of elevator proteins by targeting their linkers.
HostingRepositoryPRIDE
AnnounceDate2024-10-17
AnnouncementXMLSubmission_2024-10-17_03:37:46.388.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJulian Langer
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListNo PTMs are included in the dataset
InstrumentSynapt MS
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-07-30 07:25:39ID requested
12024-10-17 03:37:47announced
Publication List
Kuhn BT, Z, ö, ller J, Zimmermann I, Gemeinhardt T, Ö, zkul DH, Langer JD, Seeger MA, Geertsma ER, Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA. Nat Commun, 15(1):7518(2024) [pubmed]
10.1038/s41467-024-51814-8;
Keyword List
submitter keyword: HDX-MS, E. coli, UraA
Contact List
Julian D. Langer
contact affiliationProteomics, Max Planck Institute of Biophysics, Frankfurt am Main, Germany
contact emailjulian.langer@biophys.mpg.de
lab head
Julian Langer
contact affiliationMPIs for Biophysics and Brain Research
contact emailjulian.langer@biophys.mpg.de
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
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