Evidence map›Paper›PMID 28422165›Full record

ArticleScientific reports2017

Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody.

Camilo Perez, Martin Köhler, Daniel Janser, Els Pardon, Jan Steyaert, Renato Zenobi, Kaspar P Locher

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Mass Photometry Analysis of Membrane Proteins in Detergent Micelles.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. 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

7 authors.

Camilo PerezDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
Martin KöhlerDepartment of Chemistry and Applied Biosciences, ETH Zürich, CH-8093 Zürich, Switzerland.
Daniel JanserDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
Els PardonVIB Center for Structural Biology, VIB, 1050 Brussels, Belgium.
Jan SteyaertVIB Center for Structural Biology, VIB, 1050 Brussels, Belgium.
Renato ZenobiDepartment of Chemistry and Applied Biosciences, ETH Zürich, CH-8093 Zürich, Switzerland.
Kaspar P LocherDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PglK is an ABC transporter that flips a lipid-linked oligosaccharide (LLO) that serves as a donor in protein N-glycosylation. Previous structures revealed two inward-facing conformations, both with very large separations of the nucleotide binding domains (NBDs), and a closed, ADP-bound state that featured an occluded cavity. To investigate additional states, we developed conformation-sensitive, single-domain camelid nanobodies (Nb) and studied their effect on PglK activity. Biochemical, structural, and mass spectrometric analyses revealed that one inhibitory Nb binds as a single copy to homodimeric PglK. The co-crystal structure of this Nb and ADP-bound PglK revealed a new, narrowly inward-open conformation. Rather than inducing asymmetry in the PglK homodimer, the binding of one Nb results in steric constraints that prevent a second Nb to access the symmetry-related site in PglK. The Nb performed its inhibitory role by a "sticky-doorstop" mechanism, where inhibition of ATP hydrolysis and LLO flipping activity occurs due to impaired closing of the NBD interface, which prevents PglK from converting to an outward-open conformation. This inhibitory mode suggests tight conformational coupling between the ATPase sites, which may apply to other ABC transporters.

Indexed as

Protein MultimerizationAntibodies, BacterialATP-Binding Cassette TransportersBacterial ProteinsCampylobacter jejuniProtein Structure, QuaternarySingle-Domain AntibodiesAntibodies, BacterialATP-Binding Cassette TransportersBacterial ProteinsSingle-Domain Antibodies

Identifiers

PMID28422165
PMCPMC5395944

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Registered trials

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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.