Evidence map›Paper›PMID 27161977›Full record

ArticleStructure (London, England : 1993)2016

Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.

Istvan Botos, Nadim Majdalani, Stephen J Mayclin, Jennifer Gehret McCarthy, Karl Lundquist, Damian Wojtowicz, Travis J Barnard, James C Gumbart, Susan K Buchanan

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing 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

102 citing papers in PubMed.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. mBio · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Small siphophage binding to an open state of the LptDE outer membrane lipopolysaccharide translocon.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. Analysis ofmSphere · 2025
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Istvan Botos *Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Nadim Majdalani *Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Stephen J Mayclin *Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Jennifer Gehret McCarthy *Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Karl LundquistSchool of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Damian WojtowiczNational Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20892 USA.
Travis J BarnardLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
James C GumbartSchool of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Susan K BuchananLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Funding

Structural characterization of outer membrane proteins from Yersinia pestisZIADK011011 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.1M
Intramural NIH HHS ZIA DK011011
6 · The paper itself

Abstract

Incorporation of lipopolysaccharide (LPS) into the outer membrane of Gram-negative bacteria is essential for viability, and is accomplished by a two-protein complex called LptDE. We solved crystal structures of the core LptDE complexes from Yersinia pestis, Klebsiella pneumoniae, Pseudomonas aeruginosa, and a full-length structure of the K. pneumoniae LptDE complex. Our structures adopt the same plug and 26-strand β-barrel architecture found recently for the Shigella flexneri and Salmonella typhimurium LptDE structures, illustrating a conserved fold across the family. A comparison of the only two full-length structures, SfLptDE and our KpLptDE, reveals a 21° rotation of the LptD N-terminal domain that may impart flexibility on the trans-envelope LptCAD scaffold. Utilizing mutagenesis coupled to an in vivo functional assay and molecular dynamics simulations, we demonstrate the critical role of Pro231 and Pro246 in the function of the LptD lateral gate that allows partitioning of LPS into the outer membrane.

Indexed as

Bacterial Outer Membrane ProteinsBinding SitesCrystallography, X-RayGram-Negative BacteriaLipopolysaccharidesModels, MolecularProtein BindingProtein DomainsProtein Structure, SecondaryBacterial Outer Membrane ProteinsLipopolysaccharides

Identifiers

PMID27161977
PMCPMC4899211

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.