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PXD046606

PXD046606 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleUnderstanding the interaction of SurA and BAM in the outer membrane of E. coli
DescriptionThe outer membrane (OM) is a formidable barrier that protects Gram-negative bacteria against environmental threats. The correct folding and insertion of outer membrane proteins (OMPs) into the OM requires the essential OM-embedded β-barrel assembly machinery (BAM), a heptameric protein complex in E. coli. OMPs are delivered to BAM by the periplasmic chaperone SurA. However, how the activity of SurA and BAM are coordinated to ensure successful OMP delivery to BAM for folding into the OM remained unclear. We have trapped SurA in the act of OMP delivery to BAM and, via cryoEM, solved the structures of this assembly. By mutating key interaction sites we validate this interaction and use proteomics to determine how this perturbs the proteome of E. coli.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_07:00:17.115.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAntonio Calabrese
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Eclipse
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-11-02 04:07:03ID requested
12024-10-01 08:38:30announced
22024-10-22 07:00:18announced2024-10-22: Updated project metadata.
Publication List
Fenn KL, Horne JE, Crossley JA, B, ö, hringer N, Horne RJ, Sch, ä, berle TF, Calabrese AN, Radford SE, Ranson NA, Outer membrane protein assembly mediated by BAM-SurA complexes. Nat Commun, 15(1):7612(2024) [pubmed]
10.1038/s41467-024-51358-x;
Keyword List
submitter keyword: BAM,E coli, SurA, outer membrane
Contact List
Antonio Calabrese
contact affiliationAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom
contact emaila.calabrese@leeds.ac.uk
lab head
Antonio Calabrese
contact affiliationSchool of Molecular and Cellular Biology, University of Leeds
contact emaila.calabrese@leeds.ac.uk
dataset submitter
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Dataset FTP location
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