Evidence map›Paper›PMID 24108127›Full record

ArticleThe Journal of biological chemistry2013

Structure of the bacterial deacetylase LpxC bound to the nucleotide reaction product reveals mechanisms of oxyanion stabilization and proton transfer.

Gina M Clayton, Daniel J Klein, Keith W Rickert, Sangita B Patel, Maria Kornienko, Joan Zugay-Murphy, John C Reid, Srivanya Tummala, Sujata Sharma, Sheo B Singh and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Dual function of LapB (YciM) in regulatingProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Signaling through theJournal of bacteriology · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Structure, inhibition, and regulation of essential lipid A enzymes.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  19. Article
  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

13 authors at 2 institutions in 1 country.

Gina M ClaytonGlobal Structural Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486.
Daniel J KleinGlobal Structural Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486.
Keith W RickertScreening and Protein Sciences, Merck Research Laboratories, West Point, Pennsylvania 19486.
Sangita B PatelGlobal Structural Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486.
Maria KornienkoScreening and Protein Sciences, Merck Research Laboratories, West Point, Pennsylvania 19486.
Joan Zugay-MurphyScreening and Protein Sciences, Merck Research Laboratories, West Point, Pennsylvania 19486.
John C ReidGlobal Structural Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486.
Srivanya TummalaScreening and Protein Sciences, Merck Research Laboratories, West Point, Pennsylvania 19486.
Sujata SharmaScreening and Protein Sciences, Merck Research Laboratories, West Point, Pennsylvania 19486.
Sheo B SinghDiscovery Chemistry, Merck Research Laboratories, Kenilworth, New Jersey 07033.
Lynn MieselInfectious Diseases, Merck Research Laboratories, Kenilworth, New Jersey 07033.
Kevin J LumbScreening and Protein Sciences, Merck Research Laboratories, West Point, Pennsylvania 19486.
Stephen M SoissonGlobal Structural Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486. Electronic address: stephen_soisson@merck.com.
United States Military Academy · USMerck & Co., Inc., Rahway, NJ, USA (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The emergence of antibiotic-resistant strains of pathogenic bacteria is an increasing threat to global health that underscores an urgent need for an expanded antibacterial armamentarium. Gram-negative bacteria, such as Escherichia coli, have become increasingly important clinical pathogens with limited treatment options. This is due in part to their lipopolysaccharide (LPS) outer membrane components, which dually serve as endotoxins while also protecting Gram-negative bacteria from antibiotic entry. The LpxC enzyme catalyzes the committed step of LPS biosynthesis, making LpxC a promising target for new antibacterials. Here, we present the first structure of an LpxC enzyme in complex with the deacetylation reaction product, UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine. These studies provide valuable insight into recognition of substrates and products by LpxC and a platform for structure-guided drug discovery of broad spectrum Gram-negative antibiotics.

Indexed as

ProtonsAmidohydrolasesCrystallography, X-RayEscherichia coliLipopolysaccharidesMyristic AcidsProtein Structure, TertiaryUridine Diphosphate N-AcetylglucosamineAmidohydrolasesLipopolysaccharidesMyristic AcidsProtonsUDP-3-O-(3-hydroxymyristoyl)-N-acetylglucosamineUDP-3-O-acyl-N-acetylglucosamine deacetylaseUridine Diphosphate N-AcetylglucosamineAntibioticsEscherichia coliLipopolysaccharide (LPS)LpxCProtein StructureUDPX-ray Crystallography

Identifiers

PMID24108127
PMCPMC3837148
OpenAlexW2113038839

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.