Evidence map›Paper›PMID 30044025›Full record

ArticleMolecular microbiology2018

Induced conformational changes activate the peptidoglycan synthase PBP1B.

Alexander J F Egan, Roberto Maya-Martinez, Isabel Ayala, Catherine M Bougault, Manuel Banzhaf, Eefjan Breukink, Waldemar Vollmer, Jean-Pierre Simorre

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 47 citations in OpenAlex.

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  17. The LpoA activator is required to stimulate the peptidoglycan polymerase activity of its cognate cell wall synthase PBP1a.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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 4 institutions in 4 countries.

Alexander J F EganThe Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
Roberto Maya-MartinezInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CNRS, CEA, 71 avenue des Martyrs, 38000, Grenoble, France.
Isabel AyalaInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CNRS, CEA, 71 avenue des Martyrs, 38000, Grenoble, France.
Catherine M BougaultInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CNRS, CEA, 71 avenue des Martyrs, 38000, Grenoble, France.
Manuel BanzhafEuropean Molecular Biology Laboratory Heidelberg, Genome Biology Unit, Meyerhofstraße 1, 69117, Heidelberg, Germany.
Eefjan BreukinkBijvoet Center for Biomolecular Research, Department of Biochemistry of Membranes, University of Utrecht, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Waldemar VollmerThe Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
Jean-Pierre SimorreInstitut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CNRS, CEA, 71 avenue des Martyrs, 38000, Grenoble, France.ORCID 0000-0002-7943-1342
Centre National de la Recherche Scientifique · FRNewcastle University · GBEuropean Molecular Biology Laboratory · DEUtrecht University · NL

Funding

Medical Research Council MR/N501840/1Wellcome TrustWellcome Trust 101824
6 · The paper itself

Abstract

Bacteria surround their cytoplasmic membrane with an essential, stress-bearing peptidoglycan (PG) layer consisting of glycan chains linked by short peptides into a mesh-like structure. Growing and dividing cells expand their PG layer using inner-membrane anchored PG synthases, including Penicillin-binding proteins (PBPs), which participate in dynamic protein complexes to facilitate cell wall growth. In Escherichia coli, and presumably other Gram-negative bacteria, growth of the mainly single layered PG is regulated by outer membrane-anchored lipoproteins. The lipoprotein LpoB is required to activate PBP1B, which is a major, bi-functional PG synthase with glycan chain polymerising (glycosyltransferase) and peptide cross-linking (transpeptidase) activities. In this work we show how the binding of LpoB to the regulatory UB2H domain of PBP1B activates both activities. Binding induces structural changes in the UB2H domain, which transduce to the two catalytic domains by distinct allosteric pathways. We also show how an additional regulator protein, CpoB, is able to selectively modulate the TPase activation by LpoB without interfering with GTase activation.

Indexed as

Allosteric RegulationBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsMembrane ProteinsPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferaseProtein BindingProtein ConformationSerine-Type D-Ala-D-Ala CarboxypeptidaseBacterial Outer Membrane ProteinsEscherichia coli ProteinsLpoB protein, E coliMembrane Proteinspenicillin-binding protein 1B, E coliPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferaseSerine-Type D-Ala-D-Ala CarboxypeptidaseYbgF protein, E coli

Identifiers

PMID30044025
PMCPMC6220978
OpenAlexW2883126420

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.