Evidence map›Paper›PMID 33443152›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Cryo-EM structure of the full-length WzmWzt ABC transporter required for lipid-linked O antigen transport.

Christopher A Caffalette, Jochen Zimmer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  6. Article
  7. Article
  8. The role of ABC transporter DrrABC in the export of PDIM inCell surface (Amsterdam, Netherlands) · 2024
    Article
  9. Article
  10. Identification of a second glycoform of the clinically prevalent O1 antigen fromProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Lipid Transport Across Bacterial Membranes.Annual review of cell and developmental biology · 2022
    Review
  13. Single-molecule investigations of single-chain cellulose biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Article
  16. Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022
    Review
  17. Frontiers in microbiology · 2022
    Article
  18. Article
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

2 authors at 1 institution in 1 country.

Christopher A CaffaletteMolecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908.ORCID 0000-0003-1299-6485
Jochen ZimmerMolecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908 jochen_zimmer@virginia.edu.ORCID 0000-0002-8423-2882
University 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 GM008136
6 · The paper itself

Abstract

O antigens are important cell surface polysaccharides in gram-negative bacteria where they extend core lipopolysaccharides in the extracellular leaflet of the outer membrane. O antigen structures are serotype specific and form extended cell surface barriers endowing many pathogens with survival benefits. In the ABC transporter-dependent biosynthesis pathway, O antigens are assembled on the cytosolic side of the inner membrane on a lipid anchor and reoriented to the periplasmic leaflet by the channel-forming WzmWzt ABC transporter for ligation to the core lipopolysaccharides. In many cases, this process depends on the chemical modification of the O antigen's nonreducing terminus, sensed by WzmWzt via a carbohydrate-binding domain (CBD) that extends its nucleotide-binding domain (NBD). Here, we provide the cryo-electron microscopy structure of the full-length WzmWzt transporter from

Indexed as

Adenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsBinding SitesBiological TransportCell MembraneCryoelectron MicroscopyHydrolysisLipopolysaccharidesO AntigensPeriplasmProtein DomainsAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsLipopolysaccharidesO AntigensWzt protein, bacteriaABC transporterendotoxingram-negative bacterialipopolysaccharideO antigen

Identifiers

PMID33443152
PMCPMC7817213
OpenAlexW3117619993

What OpenQuestion holds

Textmetadata
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.