Evidence map›Paper›PMID 25800555›Full record

ArticleStructure (London, England : 1993)2015

Observing a lipid-dependent alteration in single lactose permeases.

Tetiana Serdiuk, Junichi Sugihara, Stefania A Mari, H Ronald Kaback, Daniel J Müller

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Complete topology inversion can be part of normal membrane protein biogenesis.Protein science : a publication of the Protein Society · 2017
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Tetiana SerdiukDepartment of Biosystems Science and Engineering, ETH Zurich, 4058 Basel, Switzerland.
Junichi SugiharaDepartment of Physiology, University of California, Los Angeles, CA 90095, USA.
Stefania A MariDepartment of Biosystems Science and Engineering, ETH Zurich, 4058 Basel, Switzerland.
H Ronald KabackDepartment of Physiology, University of California, Los Angeles, CA 90095, USA; Department of Microbiology, Immunology & Molecular Genetics, University of California, Los Angeles, CA 90095, USA; Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA. Electronic address: rkaback@mednet.ucla.edu.
Daniel J MüllerDepartment of Biosystems Science and Engineering, ETH Zurich, 4058 Basel, Switzerland. Electronic address: daniel.mueller@bsse.ethz.ch.
ETH Zurich · CHUniversity of California, Los Angeles · US

Funding

Yeast ExpressionP50GM073210 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2004 to 2013
$21.5M
NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Structural Basis for Mechanism of Secondary TransportersR01DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2005 to 2013
$3.7M
Structural Basis for Mechanism of Secondary TransportersR56DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2009 to 2009
$500k
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
NIDDK NIH HHS DK069463NIDDK NIH HHS DK51131NIDDK NIH HHS R01 DK051131NIDDK NIH HHS R01 DK069463NIDDK NIH HHS R56 DK051131NIDDK NIH HHS R56 DK069463NIGMS NIH HHS GM073210NIGMS NIH HHS P50 GM073210
6 · The paper itself

Abstract

Lipids of the Escherichia coli membrane are mainly composed of 70%-80% phosphatidylethanolamine (PE) and 20%-25% phosphatidylglycerol (PG). Biochemical studies indicate that the depletion of PE causes inversion of the N-terminal helix bundle of the lactose permease (LacY), and helix VII becomes extramembranous. Here we study this phenomenon using single-molecule force spectroscopy, which is sensitive to the structure of membrane proteins. In PE and PG at a ratio of 3:1, ∼95% of the LacY molecules adopt a native structure. However, when PE is omitted and the membrane contains PG only, LacY almost equally populates a native and a perturbed conformation. The most drastic changes occur at helices VI and VII and the intervening loop. Since helix VII contains Asp237 and Asp240, zwitterionic PE may suppress electrostatic repulsion between LacY and PG in the PE:PG environment. Thus, PE promotes a native fold and prevents LacY from populating a functionally defective, nonnative conformation.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceEscherichia coli ProteinsMembrane LipidsMolecular Sequence DataMonosaccharide Transport ProteinsProtein Structure, TertiarySymportersEscherichia coli ProteinsLacY protein, E coliMembrane LipidsMonosaccharide Transport ProteinsSymporters

Identifiers

PMID25800555
PMCPMC4394043
OpenAlexW2016841333

What OpenQuestion holds

Textmetadata
LicenceTDM
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.