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ProteomicsIdentification of SurA inter-domain dynamics and client binding by XL-MS
We present XL-MS data of apo-SurA and SurA in complex with OmpX to define (1) interdomain interactions in the periplasmic chaperone SurA, and (2) the binding site of OmpX on SurA.
ORGANISM(S): Escherichia coli 
2020-05-22 | PXD016993 | Pride
E coli Xl-ms Sura Ompx 
ProteomicsHDX-MS data of BAM and SurA binding
We present HDX-MS data of the BAM:SurA complex to define the interaction sites for SurA on BAM and vice versa.
ORGANISM(S): Escherichia coli 
2022-07-12 | PXD030268 | Pride
Bam E coli Sura Hdx-ms 
ProteomicsInter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients revealed by HDX-MS
We present HDX-MS data of apo-SurA, SurA in complex with OmpX, OmpF and a peptide with sequence WEYIPNV to define (1) interdomain dynamics in the periplasmic chaperone SurA, and (2) the binding site of OmpX, OmpF and WEYIPNV on SurA.
ORGANISM(S): Escherichia coli 
2020-05-22 | PXD017010 | Pride
E coli Hydrogen-deuterium exchange Chaperone Sura 
ProteomicsXL-MS data of BAM and SurA binding
We present XL-MS data of the BAM:SurA complex to define the interaction sites for SurA on BAM
ORGANISM(S): Escherichia coli 
2022-07-12 | PXD030209 | Pride
Bam E coli Crosslinking Sura 
ProteomicsUnderstanding the interaction of SurA and BAM in the outer membrane of E. coli
The 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....
ORGANISM(S): Escherichia coli 
2024-10-01 | PXD046606 | Pride
Bam E coli Sura Outer membrane 
GenomicsRaw genome sequence data for Acinetobacter baumannii AB5075 and the gene deletion strains SurA+Skp, SurA+DegPm Skp+DegP and SurA+Skp+DegP
The role of the periplasmic chaperones SurA, Skp and DegP for fitness, outer membrane integrity and virulence of Acinetobacter baumannii AB5075: same-same, but different?
PRJEB40766 | ENA
ProteomicsRole of SurA, BamB, BamC and HlpA for shaping the outer membrane protein composition of Pseudomonas aeruginosa
Pseudomonas aeruginosa (Pa) is one of the main causative agents of nosocomial infections and the spread of multidrug-resistant strains is rising. The outer membrane composition of Pa restricts antibiotic entry and determines virulence. For efficient outer membrane protein biogenesis, the BAM complex...
ORGANISM(S): Pseudomonas aeruginosa 
2019-03-12 | PXD011849 | Pride
Hlpa Cell surface molecules Outer membrane protein biogenesis Bamb Bamc Pseudomonas aeruginosa Bacterial infection Sura 
UnknownOuter membrane protein assembly mediated by BAM-SurA complexes.
Not available
S-EPMC11366764 | biostudies-literature
UnknownDual client binding sites in the ATP-independent chaperone SurA.
Not available
S-EPMC11401910 | biostudies-literature
UnknownDemarcating SurA activities required for outer membrane targeting of Yersinia pseudotuberculosis adhesins.
Not available
S-EPMC3697617 | biostudies-literature
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