Evidence map›Paper›PMID 30093673›Full record

ArticleNature communications2018

Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.

Cécile Morlot, Daniel Straume, Katharina Peters, Olav A Hegnar, Nolwenn Simon, Anne-Marie Villard, Carlos Contreras-Martel, Francisco Leisico, Eefjan Breukink, Christine Gravier-Pelletier and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Molecular action of NZ2114, a superior plectasin derivative.npj antimicrobials and resistance · 2026
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  16. Characterization of the MurT/GatD complex inJAC-antimicrobial resistance · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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

15 authors at 5 institutions in 5 countries.

Cécile MorlotUniversité Grenoble Alpes, CNRS, CEA, IBS UMR 5075, 38044, Grenoble, France.
Daniel StraumeFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, 1432, Norway.ORCID http://orcid.org/0000-0002-5222-9275
Katharina PetersCentre for Bacterial Cell Biology, Institute for Cell and Molecular Bioscience, Newcastle University, Newcastle Upon Tyne, NE2 4AX, United Kingdom.
Olav A HegnarFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, 1432, Norway.
Nolwenn SimonUniversité Grenoble Alpes, CNRS, CEA, IBS UMR 5075, 38044, Grenoble, France.
Anne-Marie VillardUniversité Grenoble Alpes, CNRS, CEA, IBS UMR 5075, 38044, Grenoble, France.
Carlos Contreras-MartelUniversité Grenoble Alpes, CNRS, CEA, IBS UMR 5075, 38044, Grenoble, France.
Francisco LeisicoDepartamento de Química, Universidade Nova de Lisboa, Caparica, 2829-516, Portugal.ORCID http://orcid.org/0000-0002-4672-4659
Eefjan BreukinkMembrane Biochemistry and Biophysics, Department of Chemistry, Faculty of Science, Utrecht University, Utrecht, 3584, The Netherlands.ORCID http://orcid.org/0000-0002-7311-0660
Christine Gravier-PelletierUniversité Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques UMR 8601 CNRS, Sorbonne Paris Cité (USPC), Paris, 75006, France.ORCID http://orcid.org/0000-0002-5946-9722
Laurent Le CorreUniversité Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques UMR 8601 CNRS, Sorbonne Paris Cité (USPC), Paris, 75006, France.
Waldemar VollmerCentre for Bacterial Cell Biology, Institute for Cell and Molecular Bioscience, Newcastle University, Newcastle Upon Tyne, NE2 4AX, United Kingdom.
Nicolas PietrancostaUniversité Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques UMR 8601 CNRS, Sorbonne Paris Cité (USPC), Paris, 75006, France.
Leiv Sigve HåvarsteinFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, 1432, Norway.
André ZapunUniversité Grenoble Alpes, CNRS, CEA, IBS UMR 5075, 38044, Grenoble, France. andre.zapun@ibs.fr.
Centre National de la Recherche Scientifique · FRNorwegian University of Life Sciences · NONewcastle University · GBUniversidade Nova de Lisboa · PTUtrecht University · NL

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-10-INSB-05-02Agence Nationale de la Recherche (French National Research Agency) ANR-10-LABX-49-01Wellcome TrustWellcome Trust grant 101824/Z/13/Z
6 · The paper itself

Abstract

The universality of peptidoglycan in bacteria underlies the broad spectrum of many successful antibiotics. However, in our times of widespread resistance, the diversity of peptidoglycan modifications offers a variety of new antibacterials targets. In some Gram-positive species such as Streptococcus pneumoniae, Staphylococcus aureus, or Mycobacterium tuberculosis, the second residue of the peptidoglycan precursor, D-glutamate, is amidated into iso-D-glutamine by the essential amidotransferase MurT/GatD complex. Here, we present the structure of this complex at 3.0 Å resolution. MurT has central and C-terminal domains similar to Mur ligases with a cysteine-rich insertion, which probably binds zinc, contributing to the interface with GatD. The mechanism of amidation by MurT is likely similar to the condensation catalyzed by Mur ligases. GatD is a glutaminase providing ammonia that is likely channeled to the MurT active site through a cavity network. The structure and assay presented here constitute a knowledge base for future drug development studies.

Indexed as

Anti-Bacterial AgentsBacterial ProteinsCatalytic DomainCell WallGlutamic AcidGlutaminaseGlutamineLipidsMycobacterium tuberculosisOxidoreductasesPeptidoglycanProtein DomainsStaphylococcal InfectionsStaphylococcus aureusStreptococcus pneumoniaeSulfhydryl CompoundsAnti-Bacterial AgentsBacterial ProteinsGlutamic AcidGlutaminaseGlutamineLipidsOxidoreductasesPeptidoglycanSulfhydryl Compounds

Identifiers

PMID30093673
PMCPMC6085368
OpenAlexW2885468091

What OpenQuestion holds

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LicenceCC BY
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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.