Evidence map›Paper›PMID 25402482›Full record

ArticleNature structural & molecular biology2014

Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.

Vladimir M Korkhov, Samantha A Mireku, Dmitry B Veprintsev, Kaspar P Locher

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Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

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  14. Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Triple resonance EPR spectroscopy determines the MnJournal of magnetic resonance (San Diego, Calif. : 1997) · 2018
    Article
  17. Vitamin BNature chemical biology · 2018
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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

4 authors.

Vladimir M Korkhov1] Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Zurich, Switzerland. [2] Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Samantha A MirekuInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Zurich, Switzerland.
Dmitry B VeprintsevLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Kaspar P LocherInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Zurich, Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reaction mechanism of BtuCD-F-catalyzed vitamin B12 transport into Escherichia coli is currently unclear. Here we present the structure of the last missing state in the form of AMP-PNP-bound BtuCD, trapped by a disulfide cross-link. Our structural and biochemical data allow a consistent mechanism to be formulated, thus rationalizing the roles of substrate, ATP and substrate-binding protein.

Indexed as

Adenosine TriphosphateAdenylyl ImidodiphosphateATP-Binding Cassette TransportersBiological TransportCrystallography, X-RayEscherichia coliEscherichia coli ProteinsMolecular Docking SimulationPeriplasmic Binding ProteinsProtein BindingProtein ConformationVitamin B 12Adenosine TriphosphateAdenylyl ImidodiphosphateATP-Binding Cassette TransportersBtuC peptide, E coliBtuD peptide, E colibtuF protein, E coliEscherichia coli ProteinsPeriplasmic Binding ProteinsVitamin B 12

Identifiers

PMID25402482

What OpenQuestion holds

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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.