Evidence map›Paper›PMID 28974686›Full record

ArticleNature communications2017

Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex.

Carlos Contreras-Martel, Alexandre Martins, Chantal Ecobichon, Daniel Maragno Trindade, Pierre-Jean Matteï, Samia Hicham, Pierre Hardouin, Meriem El Ghachi, Ivo G Boneca, Andréa Dessen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.4field-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

44 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  3. A broadly conserved gram-positive lipoprotein regulates cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. CoccoidVirulence · 2025
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  8. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  9. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  10. Article
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  12. Comprehensive understanding of the mutant 'giant'Frontiers in plant science · 2024
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Architecture and genomic arrangement of the MurE-MurF bacterial cell wall biosynthesis complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. A conserved zinc-binding site inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Plasticity in the cell division processes of obligate intracellular bacteria.Frontiers in cellular and infection microbiology · 2023
    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

10 authors at 3 institutions in 2 countries.

Carlos Contreras-MartelUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Bacterial Pathogenesis Group, F-38000, Grenoble, France.
Alexandre MartinsUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Bacterial Pathogenesis Group, F-38000, Grenoble, France.
Chantal EcobichonInstitut Pasteur, Unit of Biology and Genetics of the Bacterial Cell Wall, F-75015, Paris, France.
Daniel Maragno TrindadeBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas, São Paulo, 13084-971, Brazil.ORCID http://orcid.org/0000-0002-8005-8784
Pierre-Jean MatteïUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Bacterial Pathogenesis Group, F-38000, Grenoble, France.
Samia HichamInstitut Pasteur, Unit of Biology and Genetics of the Bacterial Cell Wall, F-75015, Paris, France.
Pierre HardouinUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Bacterial Pathogenesis Group, F-38000, Grenoble, France.
Meriem El GhachiInstitut Pasteur, Unit of Biology and Genetics of the Bacterial Cell Wall, F-75015, Paris, France.
Ivo G BonecaInstitut Pasteur, Unit of Biology and Genetics of the Bacterial Cell Wall, F-75015, Paris, France. ivo.gomperts-boneca@pasteur.fr.
Andréa DessenUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Bacterial Pathogenesis Group, F-38000, Grenoble, France. andrea.dessen@ibs.fr.
Centre National de la Recherche Scientifique · FRInserm · FRBrazilian Center for Research in Energy and Materials · BR

Funding

European Research Council
6 · The paper itself

Abstract

Bacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the "divisome") and lateral wall growth (the "elongasome"). MreC is a structural protein that serves as a platform during wall elongation, scaffolding other essential peptidoglycan biosynthesis macromolecules, such as penicillin-binding proteins. Despite the importance of these multi-partite complexes, details of their architecture have remained elusive due to the transitory nature of their interactions. Here, we present the crystal structures of the soluble PBP2:MreC core elongasome complex from Helicobacter pylori, and of uncomplexed PBP2. PBP2 recognizes the two-winged MreC molecule upon opening of its N-terminal region, revealing a hydrophobic zipper that serves as binding platform. The PBP2:MreC interface is essential both for protein recognition in vitro and maintenance of bacterial shape and growth. This work allows visualization as to how peptidoglycan machinery proteins are scaffolded, revealing interaction regions that could be targeted by tailored inhibitors.Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its disruption leads to loss of H. pylori shape and inability to sustain growth.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCell WallCrystallography, X-RayHelicobacter pyloriModels, MolecularPenicillin-Binding ProteinsProtein Structure, TertiarySequence AlignmentBacterial ProteinsMreC protein, BacteriaPenicillin-Binding Proteins

Identifiers

PMID28974686
PMCPMC5626683
OpenAlexW2757576334

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.