Evidence map›Paper›PMID 17927448›Full record

ArticlePLoS biology2007

Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.

Peter P Borbat, Kavitha Surendhran, Marco Bortolus, Ping Zou, Jack H Freed, Hassane S Mchaourab

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

73 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
  2. Molecular Basis for the Activation ofJournal of the American Chemical Society · 2025
    Article
  3. Article
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  10. Review
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  12. Review
  13. Spin-labeled nanobodies as protein conformational reporters for electron paramagnetic resonance in cellular membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Structural Insights into the Lipid A Transport Pathway in MsbA.Structure (London, England : 1993) · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Peter P BorbatDepartment of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York, United States of America.
Kavitha Surendhran
Marco Bortolus
Ping Zou
Jack H Freed
Hassane S Mchaourab
Vanderbilt University Medical Center · USCornell University · US

Funding

X-BAND PULSE ESR SPECTROMETER FOR STUDY OF LOW-TEMPERATURE IMPURITY-HELIUM P41RR016292 · NCRR · CORNELL UNIVERSITY ITHACA · PI GEORGIEVA, ELKA R · 2001 to 2011
$14.3M
Structural Dynamics of Multi-drug TransportersR01GM077659 · NIGMS · VANDERBILT UNIVERSITY · PI MCHAOURAB, HASSANE S · 2006 to 2023
$5.0M
ELECTRON SPIN RELAXATION IN MODEL MEMBRANESR01EB003150 · NIBIB · CORNELL UNIVERSITY ITHACA · PI FREED, JACK H · 2005 to 2016
$4.9M
TIME DOMAIN EPR SPECTROMETER: EYES10RR019120 · NCRR · VANDERBILT UNIVERSITY · PI BETH, ALBERT H · 2005 to 2005
$500k
NCRR NIH HHS P41 RR016292NCRR NIH HHS P41-RR016292NCRR NIH HHS S10 RR019120NCRR NIH HHS S10-RR019120NIBIB NIH HHS R01 EB003150NIBIB NIH HHS R01-EB03150NIGMS NIH HHS R01 GM077659NIGMS NIH HHS R01-GM077659
6 · The paper itself

Abstract

We measured the amplitude of conformational motion in the ATP-binding cassette (ABC) transporter MsbA upon lipopolysaccharide (LPS) binding and following ATP turnover by pulse double electron-electron resonance and fluorescence homotransfer. The distance constraints from both methods reveal large-scale movement of opposite signs in the periplasmic and cytoplasmic part of the transporter upon ATP hydrolysis. LPS induces distinct structural changes that are inhibited by trapping of the transporter in an ATP post-hydrolysis intermediate. The formation of this intermediate involves a 33-A distance change between the two ABCs, which is consistent with a dimerization-dissociation cycle during transport that leads to their substantial separation in the absence of nucleotides. Our results suggest that ATP-powered transport entails LPS sequestering into the open cytoplasmic chamber prior to its translocation by alternating access of the chamber, made possible by 10-20-A conformational changes.

Indexed as

Protein ConformationAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsEnergy MetabolismEscherichia coliEscherichia coli ProteinsFluorescence PolarizationHydrolysisLipopolysaccharidesModels, MolecularMutationNuclear Magnetic Resonance, BiomolecularProtein BindingSpin LabelsAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsEscherichia coli ProteinsLipopolysaccharidesMsbA protein, BacteriaSpin Labels

Identifiers

PMID17927448
PMCPMC2001213
OpenAlexW2134193705

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.