Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA from
ATP-Binding Cassette Transporters
/ metabolism
Adenosine Triphosphatases
/ metabolism
Adenosine Triphosphate
/ metabolism
Bacillus subtilis
/ metabolism
Bacterial Proteins
/ metabolism
Binding Sites
Cell Membrane
/ metabolism
Drug Resistance, Multiple
Hydrolysis
Magnesium
/ metabolism
Magnetic Resonance Spectroscopy
/ methods
Protein Conformation
Bacteria
Solid-state NMR
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
2019
2019
Historique:
received:
05
11
2018
accepted:
15
03
2019
entrez:
3
5
2019
pubmed:
3
5
2019
medline:
3
5
2019
Statut:
epublish
Résumé
ATP-binding-cassette (ABC) transporters are molecular pumps that translocate molecules across the cell membrane by switching between inward-facing and outward-facing states. To obtain a detailed understanding of their mechanism remains a challenge to structural biology, as these proteins are notoriously difficult to study at the molecular level in their active, membrane-inserted form. Here we use solid-state NMR to investigate the multidrug ABC transporter BmrA reconstituted in lipids. We identify the chemical-shift differences between the inward-facing, and outward-facing state induced by ATP:Mg
Identifiants
pubmed: 31044174
doi: 10.1038/s42003-019-0390-x
pii: 390
pmc: PMC6488656
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
Bacterial Proteins
0
Adenosine Triphosphate
8L70Q75FXE
Adenosine Triphosphatases
EC 3.6.1.-
Magnesium
I38ZP9992A
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
149Déclaration de conflit d'intérêts
The authors declare no competing interests.
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