Evidence map›Paper›PMID 23940351›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

High-resolution crystal structure reveals molecular details of target recognition by bacitracin.

Nicoleta J Economou, Simon Cocklin, Patrick J Loll

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. The Ascent of Miniproteins.Biochemistry · 2026
    Review
  3. Article
  4. Article
  5. The rise and future of peptide-based antimicrobials.Journal of microbiology (Seoul, Korea) · 2026
    Review
  6. Bacterial cell envelope-targeting antibiotics.Nature reviews. Microbiology · 2026
    Review
  7. Article
  8. Hijacking the Electron Train: Menaquinone-Binding Antimicrobial Peptides.Chembiochem : a European journal of chemical biology · 2025
    Review
  9. Article
  10. Cryo-EM structure of the conjugation H-pilus reveals the cyclic nature of the TrhA pilin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. Review
  14. TheJournal of bacteriology · 2024
    Article
  15. Review
  16. Assembly of Bacterial Surface Glycopolymers as an Antibiotic Target.Journal of microbiology (Seoul, Korea) · 2023
    Review
  17. Review
  18. Small molecule inducers of actinobacteria natural product biosynthesis.Journal of industrial microbiology & biotechnology · 2023
    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

3 authors at 1 institution in 1 country.

Nicoleta J EconomouDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USA.
Simon Cocklin
Patrick J Loll
Drexel University · US

Funding

Structural studies of target recognition by large natural product antibioticsR01GM079508 · NIGMS · DREXEL UNIVERSITY · PI LOLL, PATRICK J · 2007 to 2010
$1.2M
NIGMS NIH HHS R01 GM079508NIGMS NIH HHS R01GM079508
6 · The paper itself

Abstract

Bacitracin is a metalloantibiotic agent that is widely used as a medicine and feed additive. It interferes with bacterial cell-wall biosynthesis by binding undecaprenyl-pyrophosphate, a lipid carrier that serves as a critical intermediate in cell wall production. Despite bacitracin's broad use, the molecular details of its target recognition have not been elucidated. Here we report a crystal structure for the ternary complex of bacitracin A, zinc, and a geranyl-pyrophosphate ligand at a resolution of 1.1 Å. The antibiotic forms a compact structure that completely envelopes the ligand's pyrophosphate group, together with flanking zinc and sodium ions. The complex adopts a highly amphipathic conformation that offers clues to antibiotic function in the context of bacterial membranes. Bacitracin's efficient sequestration of its target represents a previously unseen mode for the recognition of lipid pyrophosphates, and suggests new directions for the design of next-generation antimicrobial agents.

Indexed as

Amino Acid SequenceBacitracinCell MembraneCrystallography, X-RayModels, MolecularMolecular Sequence DataPolyisoprenyl PhosphatesProtein BindingProtein ConformationSurface Plasmon ResonanceBacitracinbacitracin APolyisoprenyl Phosphatesundecaprenyl pyrophosphateantibiotic resistancemolecular recognitionX-ray crystallography

Identifiers

PMID23940351
PMCPMC3761639
OpenAlexW2072108430

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.