Evidence map›Paper›PMID 28869968›Full record

ArticleNature2017

Structural basis of MsbA-mediated lipopolysaccharide transport.

Wei Mi, Yanyan Li, Sung Hwan Yoon, Robert K Ernst, Thomas Walz, Maofu Liao

Abstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.

0numbers the graph read from it
0cells of the map it votes in
148citing 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

148 citing papers in PubMed.

  1. Article
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  9. A dual sensor regulates P-glycoprotein's structural plasticity.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Article
  12. Molecular Basis for the Activation ofJournal of the American Chemical Society · 2025
    Article
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88 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Wei MiDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Yanyan LiState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Sung Hwan YoonDepartment of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, Maryland 21201, USA.
Robert K ErnstDepartment of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, Maryland 21201, USA.
Thomas WalzLaboratory of Molecular Electron Microscopy, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA.
Maofu LiaoDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Funding

Molecular Mechanisms of Lipopolysaccharide Transport Driven by ABC TransportersR01GM122797 · NIGMS · HARVARD MEDICAL SCHOOL · PI LIAO, MAOFU · 2017 to 2021
$1.7M
NIGMS NIH HHS R01 GM122797
6 · The paper itself

Abstract

Lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria is critical for the assembly of their cell envelopes. LPS synthesized in the cytoplasmic leaflet of the inner membrane is flipped to the periplasmic leaflet by MsbA, an ATP-binding cassette transporter. Despite substantial efforts, the structural mechanisms underlying MsbA-driven LPS flipping remain elusive. Here we use single-particle cryo-electron microscopy to elucidate the structures of lipid-nanodisc-embedded MsbA in three functional states. The 4.2 Å-resolution structure of the transmembrane domains of nucleotide-free MsbA reveals that LPS binds deep inside MsbA at the height of the periplasmic leaflet, establishing extensive hydrophilic and hydrophobic interactions with MsbA. Two sub-nanometre-resolution structures of MsbA with ADP-vanadate and ADP reveal an unprecedented closed and an inward-facing conformation, respectively. Our study uncovers the structural basis for LPS recognition, delineates the conformational transitions of MsbA to flip LPS, and paves the way for structural characterization of other lipid flippases.

Indexed as

Cryoelectron MicroscopyEscherichia coliAdenosine DiphosphateATP-Binding Cassette TransportersBacterial ProteinsBiological TransportCell MembraneHydrophobic and Hydrophilic InteractionsLipid BilayersLipopolysaccharidesModels, MolecularNanostructuresPeriplasmProtein BindingProtein DomainsAdenosine DiphosphateATP-Binding Cassette TransportersBacterial ProteinsLipid BilayersLipopolysaccharidesMsbA protein, Bacteria

Identifiers

PMID28869968
PMCPMC5759761

What OpenQuestion holds

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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.