Evidence map›Paper›PMID 30778065›Full record

ArticleNature communications2019

A lipid gating mechanism for the channel-forming O antigen ABC transporter.

Christopher A Caffalette, Robin A Corey, Mark S P Sansom, Phillip J Stansfeld, Jochen Zimmer

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. 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
7.1field-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

35 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The role of ABC transporter DrrABC in the export of PDIM inCell surface (Amsterdam, Netherlands) · 2024
    Article
  10. Article
  11. Article
  12. Alchemical Free Energy Calculations on Membrane-Associated Proteins.Journal of chemical theory and computation · 2023
    Review
  13. Article
  14. Lipid Transport Across Bacterial Membranes.Annual review of cell and developmental biology · 2022
    Review
  15. Article
  16. Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Review
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.

Christopher A CaffaletteMolecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, 22908, USA.
Robin A CoreyDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Mark S P SansomDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0001-6360-7959
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Jochen ZimmerMolecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, 22908, USA. jochen_zimmer@virginia.edu.
University of Oxford · GBUniversity of Virginia · US

Funding

TRAINING IN CELL AND MOLECULAR BIOLOGYT32GM008136 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI STUKENBERG, P. TODD · 1985 to 2020
$8.5M
Molecular mechanisms of microbial complex carbohydrate secretionR01GM129666 · NIGMS · UNIVERSITY OF VIRGINIA · PI ZIMMER, JOCHEN · 2018 to 2021
$1.1M
NIGMS NIH HHS R01 GM129666NIGMS NIH HHS T32 GM008136Wellcome Trust
6 · The paper itself

Abstract

Extracellular glycan biosynthesis is a widespread microbial protection mechanism. In Gram-negative bacteria, the O antigen polysaccharide represents the variable region of outer membrane lipopolysaccharides. Fully assembled lipid-linked O antigens are translocated across the inner membrane by the WzmWzt ABC transporter for ligation to the lipopolysaccharide core, with the transporter forming a continuous transmembrane channel in a nucleotide-free state. Here, we report its structure in an ATP-bound conformation. Large structural changes within the nucleotide-binding and transmembrane regions push conserved hydrophobic residues at the substrate entry site towards the periplasm and provide a model for polysaccharide translocation. With ATP bound, the transporter forms a large transmembrane channel with openings toward the membrane and periplasm. The channel's periplasmic exit is sealed by detergent molecules that block solvent permeation. Molecular dynamics simulation data suggest that, in a biological membrane, lipid molecules occupy this periplasmic exit and prevent water flux in the transporter's resting state.

Indexed as

Adenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsCrystallography, X-RayMolecular Dynamics SimulationO AntigensProtein ConformationProtein DomainsWaterAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsO AntigensWater

Identifiers

PMID30778065
PMCPMC6379404
OpenAlexW2913394885

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.