Evidence map›Paper›PMID 24362024›Full record

ArticleThe Journal of biological chemistry2014

Conformational cycle of the vitamin B12 ABC importer in liposomes detected by double electron-electron resonance (DEER).

Benesh Joseph, Vladimir M Korkhov, Maxim Yulikov, Gunnar Jeschke, Enrica Bordignon

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
11.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 57 citations in OpenAlex.

  1. GdJournal of the American Chemical Society · 2023
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  8. Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation.Proceedings of the National Academy of Sciences of the United States of America · 2017
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  12. Coherent pump pulses in Double Electron Electron Resonance spectroscopy.Physical chemistry chemical physics : PCCP · 2016
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  17. Histidine residues are important for preserving the structure and heme binding to the C. elegans HRG-3 heme-trafficking protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
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  20. EPR and NMR spectroscopies provide input on the coordination of Cu(I) and Ag(I) to a disordered methionine segment.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Benesh JosephFrom the Laboratory of Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10 and.
Vladimir M Korkhov
Maxim Yulikov
Gunnar Jeschke
Enrica Bordignon
ETH Zurich · CHInstitute of Molecular Biology and Biophysics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Double electron-electron resonance is used here to investigate intermediates of the transport cycle of the Escherichia coli vitamin B12 ATP-binding cassette importer BtuCD-F. Previously, we showed the ATP-induced opening of the cytoplasmic gate I in TM5 helices, later confirmed by the AMP-PNP-bound BtuCD-F crystal structure. Here, other key residues are analyzed in TM10 helices (positions 307 and 322) and in the cytoplasmic gate II, i.e. the loop between TM2 and TM3 (positions 82 and 85). Without BtuF, binding of ATP induces detectable changes at positions 307 and 85 in BtuCD in liposomes. Together with BtuF, ATP triggers the closure of the cytoplasmic gate II in liposomes (reported by both positions 82 and 85). This forms a sealed cavity in the translocation channel in agreement with the AMP-PNP·BtuCD-F x-ray structure. When vitamin B12 and AMP-PNP are simultaneously present, the extent of complex formation is reduced, but the short 82-82 interspin distance detected indicates that the substrate does not affect the closed conformation of this gate. The existence of the BtuCD-F complex under these conditions is verified with spectroscopically orthogonal nitroxide and Gd(III)-based labels. The cytoplasmic gate II remains closed also in the vanadate-trapped state, but it reopens in the ADP-bound state of the complex. Therefore, we suggest that the substrate likely trapped in ATP·BtuCD-F can be released after ATP hydrolysis but before the occluded ADP-bound conformation is reached.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateATP-Binding Cassette TransportersCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHydrolysisPeriplasmic Binding ProteinsProtein Structure, QuaternaryProtein Structure, SecondaryVitamin B 12Adenosine DiphosphateAdenosine TriphosphateATP-Binding Cassette TransportersBtuC peptide, E coliBtuD peptide, E colibtuF protein, E coliEscherichia coli ProteinsPeriplasmic Binding ProteinsVitamin B 12ABC TransporterDEERDetergentElectron Paramagnetic Resonance (EPR)LiposomesMembrane BilayerMembrane ProteinsPeldor

Identifiers

PMID24362024
PMCPMC3916522
OpenAlexW2067710356

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.