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ProteomicsDistinct dynamics upon substrate and inhibitor binding to a secondary transporter
The bacterial sugar transporter XylE is a proton-coupled symporter from the Major Facilitator Family (MFS) that has been crystalized in multiple conformations, and with both substrate xylose and inhibitor glucose bound. However, this series of static pictures does not capture the coupling between li...
ORGANISM(S): Escherichia coli 
2021-03-23 | PXD018145 | Pride
Secondary transporters Major facilitator superfamily Membrane proteins Molecular dynamics simulations Conformational dynamics Molecular transport Hydrogen-deuterium exchange mass spectrometry (hdx-ms) 
ProteomicsHDX-MS on secondary transporters
Secondary transporters undergo structural rearrangements to catalyze substrate translocation across the cell membrane – yet how such conformational changes happen within a lipid environment remains poorly understood. Here, we combine hydrogen-deuterium exchange mass spectrometry (HDX-MS) with molecu...
ORGANISM(S): Escherichia coli 
2018-10-16 | PXD011060 | Pride
Conformational dynamics Structural biology Membrane proteins Lipid-protein interactions 
ProteomicsHDX-MS of CSN-CRL2 complexes - Structural basis of Cullin 2 RING E3 ligase regulation by the COP9 signalosome
Cullin-Ring E3 Ligases (CRLs) regulate a multitude of cellular pathways through specific substrate receptors. The COP9 signalosome (CSN) deactivates CRLs by removing NEDD8 (N8) from activated Cullins. The structure of stable CSN-CRL can be used to understand this mechanism of regulation. Here we pre...
ORGANISM(S): Homo sapiens (Human) 
2019-09-13 | PXD013001 | Pride
E3 ligase Structural biology Biological Conformational dynamics Protein-protein interactions Cop9 signalosome 
ProteomicsXL-MS and Native MS for CSN-CRL2 complexes
Cullin-Ring E3 Ligases (CRLs) regulate a multitude of cellular pathways through specific substrate receptors. The COP9 signalosome (CSN) deactivates CRLs by removing NEDD8 (N8) from activated Cullins. The structure of stable CSN-CRL can be used to understand this mechanism of regulation. Here we pre...
ORGANISM(S): Homo sapiens (Human) 
2019-09-13 | PXD013018 | Pride
Xl-ms Mass spectrometry Crl2 Cop9 signalosome Native ms Cullin ring e3 ligase 
ProteomicsInvestigating the dynamics of the SecA–SecYEG complex dynamic by HDX-MS
We employ hydrogen-deuterium exchange mass spectrometry (HDX-MS) to investigate the conformational dynamics required to facilitate based Brownian ratchet mechanism for protein secretion (by the SecA-SecYEG complex).
ORGANISM(S): Escherichia coli 
2019-07-16 | PXD013594 | Pride
Seca–secyeg Hdx-ms 
ProteomicsStructural dynamics in the evolution of SARS-CoV-2 spike glycoprotein: HDX-MS analysis of the spike of the original Wuhan isolate, G614 spike mutant, and the isolated ancestral RBD - in apo state and in complex with the ACE2 receptor
The spike glycoprotein of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates binding to the ACE2 receptor and subsequent membrane fusion. It exists in a range of conformations, including a closed state unable to bind the ACE2 receptor, and an open state that does so but displa...
ORGANISM(S): Homo sapiens (Human) 
2023-03-15 | PXD039760 | Pride
Sars-cov-2 Spike glycoprotein Hdx-ms 
ProteomicsStructural dynamics in the evolution of SARS-CoV-2 spike glycoprotein: HDX-MS analysis of the spike of alpha, beta, delta and omicron variants - in apo state and in complex with the ACE2 receptor
The spike glycoprotein of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates binding to the ACE2 receptor and subsequent membrane fusion. It exists in a range of conformations, including a closed state unable to bind the ACE2 receptor, and an open state that does so but displa...
ORGANISM(S): Homo sapiens (Human) 
2023-03-15 | PXD039762 | Pride
Sars-cov-2 Spike glycoprotein Hdx-ms 
ProteomicsLigand induced conformational changes in the B1-Adrenergic Receptor Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry
Project employ Hydrogen Deuterium Exchange Mass Spectrometry (HDX-MS), to characterise the structural dynamics of turkey β1-adrenergic receptor (tβ1AR) in complex with nine ligands, including agonists, partial agonists and antagonists.We show that dynamic signatures across the GPCR structure can be ...
ORGANISM(S): Meleagris gallopavo (Common turkey) 
2024-08-30 | PXD051297 | Pride
Gpcrs B1-adrenergic receptor Hdx-ms 
ProteomicsHDX-MS reveals the perturbed structural dynamics underlie inhibition and altered specificity of the multidrug efflux pump AcrB
Perturbed structural dynamics underlie inhibition and altered specificity of the multidrug efflux pump AcrB
ORGANISM(S): Escherichia coli 
2020-10-07 | PXD019047 | Pride
Acrb Hdx-ms Membrane proteins Multi-drug efflux pumps 
ProteomicsAn Automated HDX-MS Platform for characterisation of Membrane Proteins within Biological Membranes
This project developed a fully automated hydrogen-deuterium exchange mass spectrometry (HDX-MS) platform incorporating a dual mode delipidation, using zirconium dioxide (ZrO₂) and online size-exclusion chromatography (SEC) in tandem. The platform was used to compare the conformational dynamics of th...
ORGANISM(S): Escherichia coli 
2026-10-15 | PXD084003 | Pride
Hdx-ms Delipidation 
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