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Article

Probing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site-directed spin labeling approach.

Protein science : a publication of the Protein Society - 1 Jul 2009

Do Cao Marie-Ange, Crouzy Serge, Kim Miyeon, Becchi Michel, Cafiso David S, Di Pietro Attilio, Jault Jean-Michel

Abstract excerpt

Previously published 3-D structures of a prototypic ATP-binding cassette (ABC) transporter, MsbA, have been recently corrected revealing large rigid-body motions possibly linked to its catalytic cycle. Here, a closely related multidrug bacterial ABC transporter, BmrA, was studied using site-directed spin labeling by focusing on a region connecting the transmembrane domain and the nucleotide-binding domain (NBD)....

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Share to ATP-Binding Cassette Transporters
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance, Multiple, Bacterial

Share to Electron Spin Resonance Spectroscopy

Share to Escherichia coli Proteins

Share to Mutagenesis, Site-Directed

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Share to Spin Labels

Source

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Identifiers

PMID: 19479721
DOI: 10.1002/pro.141
PMCID: PMC2775218

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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