Evidence map›Paper›PMID 29182854›Full record

ArticleJournal of the American Chemical Society2017

Identification of a Functionally Unique Family of Penicillin-Binding Proteins.

Michael A Welsh, Atsushi Taguchi, Kaitlin Schaefer, Daria Van Tyne, François Lebreton, Michael S Gilmore, Daniel Kahne, Suzanne Walker

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

41 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Activity Profiling of Mycobacterial L,D-Transpeptidases.bioRxiv : the preprint server for biology · 2026
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  3. Article
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  7. Chemical science · 2024
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  16. Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Review
  19. Article
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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

8 authors at 2 institutions in 1 country.

Michael A WelshDepartment of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.ORCID 0000-0001-8268-6285
Atsushi TaguchiDepartment of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Kaitlin SchaeferDepartment of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Daria Van TyneDepartment of Ophthalmology, Harvard Medical School, Massachusetts Eye and Ear Infirmary , Boston, Massachusetts 02114, United States.
François LebretonDepartment of Ophthalmology, Harvard Medical School, Massachusetts Eye and Ear Infirmary , Boston, Massachusetts 02114, United States.
Michael S GilmoreDepartment of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Daniel KahneDepartment of Chemistry and Chemical Biology, Harvard University , Cambridge, Massachusetts 02138, United States.ORCID 0000-0002-8296-1424
Suzanne WalkerDepartment of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.ORCID 0000-0002-0545-914X
Harvard University · USMassachusetts Eye and Ear Infirmary · US

Funding

Technical Mother Machine CoreP01AI083214 · NIAID · SCHEPENS EYE RESEARCH INSTITUTE · PI David C Hooper · 2009 to 2026
$39.4M
Targeting bacterial cell wall biogenesis for the development of novel antimicrobU19AI109764 · NIAID · HARVARD MEDICAL SCHOOL · PI KASPER, DENNIS L. · 2014 to 2018
$25.2M
Studies Toward Hybrid Glycopeptide AntibioticsR01GM066174 · NIGMS · PRINCETON UNIVERSITY · PI KAHNE, DANIEL · 2002 to 2018
$8.9M
Mechanism and Inhibition of Enzymes that Assemble Bacterial Cell WallR01GM076710 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2007 to 2019
$5.9M
Biochemical characterization of LMW PBPS with novel transpeptidase activityF32GM123579 · NIGMS · HARVARD MEDICAL SCHOOL · PI WELSH, MICHAEL AVERY · 2017 to 2019
$130k
NIAID NIH HHS P01 AI083214NIAID NIH HHS U19 AI109764NIGMS NIH HHS F32 GM123579NIGMS NIH HHS R01 GM066174NIGMS NIH HHS R01 GM076710
6 · The paper itself

Abstract

Penicillin-binding proteins (PBPs) are enzymes involved in the assembly of the bacterial cell wall, a major target for antibiotics. These proteins are classified by mass into high-molecular-weight PBPs, which are transpeptidases that form peptidoglycan cross-links, and low-molecular-weight PBPs, which are typically hydrolases. We report a functionally unique family of low-molecular-weight PBPs that act as transpeptidases rather than hydrolases, but they do not cross-link peptidoglycan. We show that these PBPs can exchange d-amino acids bearing chemical tags or affinity handles into peptidoglycan precursors, including Lipid II, enabling biochemical studies of proteins involved in cell wall assembly. We report that, in two organisms, the PBPs incorporate lysine into cellular peptidoglycan and that, further, the PBPs have the unprecedented ability to transfer the primary ε-amine of lysine to peptidoglycan.

Indexed as

AminesBacterial ProteinsCatalytic DomainCell WallEnterococcus faecalisLysineMolecular WeightPenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesStreptococcus gordoniiUridine Diphosphate N-Acetylmuramic AcidAminesBacterial ProteinsLysinemuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolPenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID29182854
PMCPMC5729098
OpenAlexW2770310439

What OpenQuestion holds

Textmetadata
LicenceTDM
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.