Evidence map›Paper›PMID 26443496›Full record

ReviewProtein science : a publication of the Protein Society2016

The AbgT family: A novel class of antimetabolite transporters.

Jared A Delmar, Edward W Yu

Open access · greenAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. TheScience advances · 2024
    Article
  7. The complete catalog of antimicrobial resistance secondary active transporters inComputational and structural biotechnology journal · 2024
    Article
  8. Review
  9. Defense mechanisms ofFrontiers in antibiotics · 2024
    Review
  10. Efflux, Signaling and Warfare in a Polymicrobial World.Antibiotics (Basel, Switzerland) · 2023
    Review
  11. Infection and drug resistance · 2023
    Article
  12. Infection-specific PET imaging withFrontiers in microbiology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. 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.

Jared A DelmarDepartment of Physics and Astronomy, Iowa State University, Ames, Iowa, 50011.
Edward W YuDepartment of Physics and Astronomy, Iowa State University, Ames, Iowa, 50011.
Iowa State University · US

Funding

Structure and mechanism of the AbgT-family transportersR01AI114629 · NIAID · IOWA STATE UNIVERSITY · PI YU, EDWARD W · 2015 to 2017
$1.1M
NIAID NIH HHS R01 AI114629NIAID NIH HHS R01AI114629
6 · The paper itself

Abstract

The AbgT family of transporters was thought to contribute to bacterial folate biosynthesis by importing the catabolite p-aminobenzoyl-glutamate for producing this essential vitamin. Approximately 13,000 putative transporters of the family have been identified. However, before our work, no structural information was available and even functional data were minimal for this family of membrane proteins. To elucidate the structure and function of the AbgT family of transporters, we recently determined the X-ray structures of the full-length Alcanivorax borkumensis YdaH and Neisseria gonorrhoeae MtrF membrane proteins. The structures reveal that these two transporters assemble as dimers with architectures distinct from all other families of transporters. Both YdaH and MtrF are bowl-shaped dimers with a solvent-filled basin extending from the cytoplasm halfway across the membrane bilayer. The protomers of YdaH and MtrF contain nine transmembrane helices and two hairpins. These structures directly suggest a plausible pathway for substrate transport. A combination of the crystal structure, genetic analysis and substrate accumulation assay indicates that both YdaH and MtrF behave as exporters, capable of removing the folate metabolite p-aminobenzoic acid from bacterial cells. Further experimental data based on drug susceptibility and radioactive transport assay suggest that both YdaH and MtrF participate as antibiotic efflux pumps, importantly mediating bacterial resistance to sulfonamide antimetabolite drugs. It is possible that many of these AbgT-family transporters act as exporters, thereby conferring bacterial resistance to sulfonamides. The AbgT-family transporters may be important targets for the rational design of novel antibiotics to combat bacterial infections.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsAntimetabolitesBacteriaBacterial ProteinsBiological TransportCrystallography, X-RayFolic AcidGene Expression Regulation, BacterialMembrane Transport ProteinsModels, MolecularMolecular Sequence DataProtein ConformationSequence AlignmentAnti-Bacterial AgentsAntimetabolitesBacterial ProteinsFolic AcidMembrane Transport ProteinsAbgT-family transportersAlcanivorax borkumensis YdaHantimetabolite transportersmembrane proteinsNeisseria gonorrhoeae MtrFX-ray crystallography

Identifiers

PMID26443496
PMCPMC4815354
OpenAlexW1852257267

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.