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HDX-MS reveals the perturbed structural dynamics underlie inhibition and altered specificity of the multidrug efflux pump AcrB

ABSTRACT: Perturbed structural dynamics underlie inhibition and altered specificity of the multidrug efflux pump AcrB

INSTRUMENT(S): Synapt MS

ORGANISM(S): Escherichia Coli

SUBMITTER: Zainab Ahdash

LAB HEAD: Argyris Politis

PROVIDER: PXD019047 | Pride | 2020-10-07

REPOSITORIES: Pride

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Perturbed structural dynamics underlie inhibition and altered efflux of the multidrug resistance pump AcrB.

Reading Eamonn E Ahdash Zainab Z Fais Chiara C Ricci Vito V Wang-Kan Xuan X Grimsey Elizabeth E Stone Jack J Malloci Giuliano G Lau Andy M AM Findlay Heather H Konijnenberg Albert A Booth Paula J PJ Ruggerone Paolo P Vargiu Attilio V AV Piddock Laura J V LJV Politis Argyris A

Nature communications 20201104 1

Resistance-nodulation-division efflux pumps play a key role in inherent and evolved multidrug resistance in bacteria. AcrB, a prototypical member of this protein family, extrudes a wide range of antimicrobial agents out of bacteria. Although high-resolution structures exist for AcrB, its conformational fluctuations and their putative role in function are largely unknown. Here, we determine these structural dynamics in the presence of substrates using hydrogen/deuterium exchange mass spectrometry ...[more]

PMID: 33149158

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