Evidence map›Paper›PMID 37833269›Full record

ArticleNature communications2023

Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410.

Sille Remm, Dario De Vecchis, Jendrik Schöppe, Cedric A J Hutter, Imre Gonda, Michael Hohl, Simon Newstead, Lars V Schäfer, Markus A Seeger

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Structure and function ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. 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

9 authors.

Sille RemmInstitute of Medical Microbiology, University of Zurich, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-5204-4556
Dario De VecchisCenter for Theoretical Chemistry, Ruhr University Bochum, Bochum, Germany.
Jendrik SchöppeInstitute of Biochemistry, University of Zurich, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-2689-5549
Cedric A J HutterInstitute of Medical Microbiology, University of Zurich, Zürich, Switzerland.
Imre GondaInstitute of Medical Microbiology, University of Zurich, Zürich, Switzerland.
Michael HohlInstitute of Medical Microbiology, University of Zurich, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-6046-4865
Simon NewsteadDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.ORCID http://orcid.org/0000-0001-7432-2270
Lars V SchäferCenter for Theoretical Chemistry, Ruhr University Bochum, Bochum, Germany. lars.schaefer@ruhr-uni-bochum.de.ORCID http://orcid.org/0000-0002-8498-3061
Markus A SeegerInstitute of Medical Microbiology, University of Zurich, Zürich, Switzerland. m.seeger@imm.uzh.ch.ORCID http://orcid.org/0000-0003-1761-8571

Funding

European Research Council consolidator grant n° 772190Swiss National Science Foundation PP00P3_144823
6 · The paper itself

Abstract

Mycobacterium tuberculosis is protected from antibiotic therapy by a multi-layered hydrophobic cell envelope. Major facilitator superfamily (MFS) transporter Rv1410 and the periplasmic lipoprotein LprG are involved in transport of triacylglycerides (TAGs) that seal the mycomembrane. Here, we report a 2.7 Å structure of a mycobacterial Rv1410 homologue, which adopts an outward-facing conformation and exhibits unusual transmembrane helix 11 and 12 extensions that protrude ~20 Å into the periplasm. A small, very hydrophobic cavity suitable for lipid transport is constricted by a functionally important ion-lock likely involved in proton coupling. Combining mutational analyses and MD simulations, we propose that TAGs are extracted from the core of the inner membrane into the central cavity via lateral clefts present in the inward-facing conformation. The functional role of the periplasmic helix extensions is to channel the extracted TAG into the lipid binding pocket of LprG.

Indexed as

Membrane Transport ProteinsMycobacterium tuberculosisBiological TransportLipidsMembranesProtein ConformationLipidsMembrane Transport Proteins

Identifiers

PMID37833269
PMCPMC10576003

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.