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

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F.

Nature - 18 Oct 2012

Korkhov Vladimir M, Mireku Samantha A, Locher Kaspar P

Abstract excerpt

The ATP-binding cassette (ABC) transporter BtuCD mediates the uptake of vitamin B(12) across the inner membrane of Escherichia coli. Previous structures have shown the conformations of apo states, but the transport mechanism has remained unclear. Here we report the 3.5 Å crystal structure of the transporter-binding protein complex BtuCD-BtuF (BtuCD-F) trapped in an β-γ-imidoadenosine 5'-phosphate (AMP-PNP)-bound...

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 ATP-Binding Cassette Transporters
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnesium

Share to Mutant Proteins

Share to Periplasmic Binding Proteins

Share to Protein Subunits

Share to Vitamin B 12

Source

Identifiers

PMID: 23000901
DOI: 10.1038/nature11442

Genes

PNP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F.PMID 23000901Read ↗

ATP binding cassette systems: structures, mechanisms, and functionsSemantic proximity Read ↗

Exploring intermolecular interactions of a substrate binding protein using a riboswitch-based sensor.Semantic proximity Read ↗

A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization.Semantic proximity Read ↗

BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B <sub>12</sub> uptake in gut <i>Bacteroides</i>Semantic proximity Read ↗

Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.Semantic proximity Read ↗

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette SystemsSemantic proximity Read ↗

Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states.Semantic proximity Read ↗

Structures of the human peroxisomal fatty acid transporter ABCD1 in a lipid environmentSemantic proximity Read ↗

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

Cryo-EM structure of the Nisin resistance pump PsdAB reveals an unusual ABC transporter architecture.Semantic proximity Read ↗

Structural basis for the mechanism of ABC transporters.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 ↗

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