Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Substrate binding stabilizes a pre-translocation intermediate in the ATP-binding cassette transport protein MsbA.

The Journal of biological chemistry - 26 Jul 2013

Doshi Rupak, van Veen Hendrik W

Abstract excerpt

ATP-binding cassette (ABC) transporters belong to one of the largest protein superfamilies that expands from prokaryotes to man. Recent x-ray crystal structures of bacterial and mammalian ABC exporters suggest a common alternating access mechanism of substrate transport, which has also been biochemically substantiated. However, the current model does not yet explain the coupling between substrate binding and ATP...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Benzimidazoles
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ethidium

Share to Fluorescence Resonance Energy Transfer

Share to Hydrolysis

Share to Protein Multimerization

Share to Verapamil

Source

Open in PubMed Open full text

Identifiers

PMID: 23766512
DOI: 10.1074/jbc.M113.485714
PMCID: PMC3724623

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substrate binding stabilizes a pre-translocation intermediate in the ATP-binding cassette transport protein MsbA.PMID 23766512Read ↗

Mapping Daunorubicin-binding Sites in the ATP-binding Cassette Transporter MsbA Using Site-specific Quenching by Spin LabelsSemantic proximity Read ↗

Molecular disruption of the power stroke in the ATP-binding cassette transport protein MsbA.Semantic proximity Read ↗

The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA.Semantic proximity Read ↗

The Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding Domains.Semantic proximity Read ↗

Probing native metal ion association sites through quenching of fluorophores in the nucleotide-binding domains of the ABC transporter MsbA.Semantic proximity Read ↗

The Lipid Bilayer Modulates the Structure and Function of an ATP-binding Cassette Exporter.Semantic proximity Read ↗

Characterization of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA.Semantic proximity Read ↗

Dissecting the Conformational Dynamics of the Bile Acid Transporter Homologue ASBTNM.Semantic proximity Read ↗

Structural insight into binding site access and ligand recognition by human ABCB1Semantic proximity Read ↗

Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.Semantic proximity Read ↗

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

Structural insights into binding-site access and ligand recognition by human ABCB1Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.