Evidence map›Paper›PMID 24821816›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Outer-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1B.

Alexander J F Egan, Nicolas L Jean, Alexandra Koumoutsi, Catherine M Bougault, Jacob Biboy, Jad Sassine, Alexandra S Solovyova, Eefjan Breukink, Athanasios Typas, Waldemar Vollmer and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.8field-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

74 citing papers in PubMed, 109 citations in OpenAlex.

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  19. Heterologous Display ofMembranes · 2023
    Article
  20. The Influence of Outer Membrane Protein on Ampicillin Resistance ofThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2023
    Article

14 more citing papers are in PubMed but not listed here.

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

11 authors at 6 institutions in 4 countries.

Alexander J F EganCentre for Bacterial Cell Biology.
Nicolas L JeanInstitut de Biologie Structurale, Université Grenoble Alpes, F-38027 Grenoble, France;Institut de Biologie Structurale, Direction des Sciences du Vivant, Commissariat à l'Energie Atomique, F-38027 Grenoble, France;Institut de Biologie Structurale, Centre National de la Recherche Scientifique, F-38027 Grenoble, France;
Alexandra KoumoutsiEuropean Molecular Biology Laboratory, Genome Biology Unit, 69117 Heidelberg, Germany; and.
Catherine M BougaultInstitut de Biologie Structurale, Université Grenoble Alpes, F-38027 Grenoble, France;Institut de Biologie Structurale, Direction des Sciences du Vivant, Commissariat à l'Energie Atomique, F-38027 Grenoble, France;Institut de Biologie Structurale, Centre National de la Recherche Scientifique, F-38027 Grenoble, France;
Jacob BiboyCentre for Bacterial Cell Biology.
Jad SassineCentre for Bacterial Cell Biology.
Alexandra S SolovyovaInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4AX, United Kingdom;
Eefjan BreukinkDepartment of Biochemistry of Membranes, Bijvoet Center for Biomolecular Research, University of Utrecht, 3584 CH, Utrecht, The Netherlands.
Athanasios TypasEuropean Molecular Biology Laboratory, Genome Biology Unit, 69117 Heidelberg, Germany; and typas@embl.de w.vollmer@ncl.ac.uk jean-pierre.simorre@ibs.fr.
Waldemar VollmerCentre for Bacterial Cell Biology, typas@embl.de w.vollmer@ncl.ac.uk jean-pierre.simorre@ibs.fr.
Jean-Pierre SimorreInstitut de Biologie Structurale, Université Grenoble Alpes, F-38027 Grenoble, France;Institut de Biologie Structurale, Direction des Sciences du Vivant, Commissariat à l'Energie Atomique, F-38027 Grenoble, France;Institut de Biologie Structurale, Centre National de la Recherche Scientifique, F-38027 Grenoble, France; typas@embl.de w.vollmer@ncl.ac.uk jean-pierre.simorre@ibs.fr.
European Molecular Biology Laboratory · DECommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInstitut de Biologie Structurale · FRNewcastle University · GBUniversité Grenoble Alpes · FRUtrecht University · NL

Funding

Biotechnology and Biological Sciences Research Council BB/I020012/1
6 · The paper itself

Abstract

Bacteria surround their cytoplasmic membrane with an essential, stress-bearing peptidoglycan (PG) layer. Growing and dividing cells expand their PG layer by using membrane-anchored PG synthases, which are guided by dynamic cytoskeletal elements. In Escherichia coli, growth of the mainly single-layered PG is also regulated by outer membrane-anchored lipoproteins. The lipoprotein LpoB is required for the activation of penicillin-binding protein (PBP) 1B, which is a major, bifunctional PG synthase with glycan chain polymerizing (glycosyltransferase) and peptide cross-linking (transpeptidase) activities. Here, we report the structure of LpoB, determined by NMR spectroscopy, showing an N-terminal, 54-aa-long flexible stretch followed by a globular domain with similarity to the N-terminal domain of the prevalent periplasmic protein TolB. We have identified the interaction interface between the globular domain of LpoB and the noncatalytic UvrB domain 2 homolog domain of PBP1B and modeled the complex. Amino acid exchanges within this interface weaken the PBP1B-LpoB interaction, decrease the PBP1B stimulation in vitro, and impair its function in vivo. On the contrary, the N-terminal flexible stretch of LpoB is required to stimulate PBP1B in vivo, but is dispensable in vitro. This supports a model in which LpoB spans the periplasm to interact with PBP1B and stimulate PG synthesis.

Indexed as

Apolipoproteins BBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsNuclear Magnetic Resonance, BiomolecularPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferasePeriplasmProtein Interaction Domains and MotifsProtein Structure, TertiarySerine-Type D-Ala-D-Ala CarboxypeptidaseApolipoproteins BBacterial Outer Membrane ProteinsEscherichia coli Proteinspenicillin-binding protein 1B, E coliPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferaseSerine-Type D-Ala-D-Ala Carboxypeptidase

Identifiers

PMID24821816
PMCPMC4050580
OpenAlexW2061772313

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.