Proteomics

Dataset Information

0

HDX-MS analysis of BAM variants


ABSTRACT: Here we present HDX-MS data to study the conformational dynamics of BAM, BAM(T434A) and BAM(LVPR).

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

SUBMITTER: Antonio Calabrese  

LAB HEAD: Antonio Calabrese

PROVIDER: PXD057055 | Pride | 2025-10-13

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Gdn_Quench_HDX.DnX Other
fbsaca_230216_HDX_BAM_Hinge_01.raw.zip Raw
fbsaca_230216_HDX_BAM_Hinge_03.raw.zip Raw
fbsaca_230216_HDX_BAM_Hinge_05.raw.zip Raw
fbsaca_230216_HDX_BAM_Hinge_07.raw.zip Raw
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Publications


The β-barrel assembly machinery (BAM) inserts β-barrel proteins into the outer membrane of Gram-negative bacteria, forming an essential permeability barrier. The core BAM component, BamA, is a β-barrel protein with an N-terminal periplasmic extension comprising five polypeptide transport-associated (POTRA) domains. Whilst BamA's structure is well characterised, it remains unclear how β-barrel and POTRA domain motions are coordinated. Using BamA variants with mutations in the hinge region between  ...[more]

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