Evidence map›Paper›PMID 24981231›Full record

ArticleThe Journal of general physiology2014

Concerted loop motion triggers induced fit of FepA to ferric enterobactin.

Chuck R Smallwood, Lorne Jordan, Vy Trinh, Daniel W Schuerch, Amparo Gala, Mathew Hanson, Matthew Hanson, Yan Shipelskiy, Aritri Majumdar, Salete M C Newton and 1 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Siderophore-mediated iron acquisition byJournal of bacteriology · 2024
    Article
  4. Article
  5. Article
  6. HDX-MS performed on BtuB inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Review
  9. Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020
    Review
  10. Article
  11. Conformational rearrangements in the N-domain ofThe Journal of biological chemistry · 2020
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
4 · The record

Corrections and comments

  • Erratum issued
    Hanson, Matthew [corrected to Hanson, Mathew]
5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Chuck R SmallwoodThe Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019.
Lorne JordanThe Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506.
Vy TrinhThe Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019.
Daniel W SchuerchThe Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019.
Amparo GalaThe Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019.
Mathew HansonThe Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506.
Matthew Hanson
Yan ShipelskiyThe Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506.
Aritri MajumdarThe Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506.
Salete M C NewtonThe Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506.
Phillip E KlebbaThe Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506 peklebba@ksu.edu.
Kansas State University · USUniversity of Oklahoma · US

Funding

LOOP DELETION MUTAGENESIS OF FEPAR01GM053836 · NIGMS · UNIVERSITY OF OKLAHOMA NORMAN · PI KLEBBA, PHILLIP E · 1995 to 2009
$2.4M
NIGMS NIH HHS GM53836NIGMS NIH HHS R01 GM053836
6 · The paper itself

Abstract

Spectroscopic analyses of fluorophore-labeled Escherichia coli FepA described dynamic actions of its surface loops during binding and transport of ferric enterobactin (FeEnt). When FeEnt bound to fluoresceinated FepA, in living cells or outer membrane fragments, quenching of fluorophore emissions reflected conformational motion of the external vestibular loops. We reacted Cys sulfhydryls in seven surface loops (L2, L3, L4, L5, L7 L8, and L11) with fluorophore maleimides. The target residues had different accessibilities, and the labeled loops themselves showed variable extents of quenching and rates of motion during ligand binding. The vestibular loops closed around FeEnt in about a second, in the order L3 > L11 > L7 > L2 > L5 > L8 > L4. This sequence suggested that the loops bind the metal complex like the fingers of two hands closing on an object, by individually adsorbing to the iron chelate. Fluorescence from L3 followed a biphasic exponential decay as FeEnt bound, but fluorescence from all the other loops followed single exponential decay processes. After binding, the restoration of fluorescence intensity (from any of the labeled loops) mirrored cellular uptake that depleted FeEnt from solution. Fluorescence microscopic images also showed FeEnt transport, and demonstrated that ferric siderophore uptake uniformly occurs throughout outer membrane, including at the poles of the cells, despite the fact that TonB, its inner membrane transport partner, was not detectable at the poles.

Indexed as

MotionBacterial Outer Membrane ProteinsCarrier ProteinsEnterobactinEscherichia coliProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportReceptors, Cell SurfaceBacterial Outer Membrane ProteinsCarrier ProteinsEnterobactinenterobactin receptorferrienterochelinReceptors, Cell Surface

Identifiers

PMID24981231
PMCPMC4076525
OpenAlexW2154309648

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.