Evidence map›Paper›PMID 34226658›Full record

ArticleCommunications biology2021

Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody.

Sushant Kumar, Arunabh Athreya, Ashutosh Gulati, Rahul Mony Nair, Ithayaraja Mahendran, Rakesh Ranjan, Aravind Penmatsa

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Review
  6. Article
  7. Article
  8. Methods for Engineering Binders to Multi-Pass Membrane Proteins.Bioengineering (Basel, Switzerland) · 2023
    Review
  9. Article
  10. Article
  11. The role of TMS 12 in the staphylococcal multidrug efflux protein QacA.The Journal of antimicrobial chemotherapy · 2023
    Article
  12. Nanobodies: Robust miniprotein binders in biomedicine.Advanced drug delivery reviews · 2023
    Review
  13. Review
  14. Review
  15. Article
  16. 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

7 authors at 6 institutions in 3 countries.

Sushant Kumar *Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.ORCID 0000-0002-0317-8520
Arunabh Athreya *Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.ORCID 0000-0003-2133-2795
Ashutosh GulatiMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.ORCID 0000-0003-0960-994X
Rahul Mony NairMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.ORCID 0000-0001-5016-743X
Ithayaraja MahendranMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Rakesh RanjanPrincipal Scientist, ICAR-National Research Centre of Camel (NRCC), Bikaner, India.ORCID 0000-0002-5849-6016
Aravind PenmatsaMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India. penmatsa@iisc.ac.in.ORCID 0000-0001-9519-5055
Indian Institute of Science Bangalore · INInternational Centre for Genetic Engineering and Biotechnology · INNational Research Centre on Camel · INStockholm University · SEVan Andel Institute · USVanderbilt University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI STEVEN E EALICK · 2018 to 2026
$34.2M
DBT-Wellcome Trust India Alliance IA/I/15/2/502063NIGMS NIH HHS P30 GM124165Wellcome Trust
6 · The paper itself

Abstract

Transporters play vital roles in acquiring antimicrobial resistance among pathogenic bacteria. In this study, we report the X-ray structure of NorC, a 14-transmembrane major facilitator superfamily member that is implicated in fluoroquinolone resistance in drug-resistant Staphylococcus aureus strains, at a resolution of 3.6 Å. The NorC structure was determined in complex with a single-domain camelid antibody that interacts at the extracellular face of the transporter and stabilizes it in an outward-open conformation. The complementarity determining regions of the antibody enter and block solvent access to the interior of the vestibule, thereby inhibiting alternating-access. NorC specifically interacts with an organic cation, tetraphenylphosphonium, although it does not demonstrate an ability to transport it. The interaction is compromised in the presence of NorC-antibody complex, consequently establishing a strategy to detect and block NorC and related transporters through the use of single-domain camelid antibodies.

Indexed as

AnimalsAnti-Bacterial AgentsBacterial ProteinsBinding SitesCrystallography, X-RayHumansMembrane Transport ProteinsModels, MolecularPhylogenyProtein BindingProtein ConformationSingle-Domain AntibodiesStaphylococcal InfectionsStaphylococcus aureusAnti-Bacterial AgentsBacterial ProteinsMembrane Transport ProteinsSingle-Domain Antibodies

Identifiers

PMID34226658
PMCPMC8257674
OpenAlexW3177827068

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.