Evidence map›Paper›PMID 29540682›Full record

ArticleNature communications2018

Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis.

Meriem El Ghachi, Nicole Howe, Chia-Ying Huang, Vincent Olieric, Rangana Warshamanage, Thierry Touzé, Dietmar Weichert, Phillip J Stansfeld, Meitian Wang, Fred Kerff and 1 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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 58 citations in OpenAlex.

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  14. Mechanistic insights into the CChemical science · 2022
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  15. Review
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  17. Mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Review
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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

11 authors at 5 institutions in 5 countries.

Meriem El GhachiCentre d'Ingénierie des Protéines, InBioS, Université de Liège, allée du 6 Août 19, Bât B5a, 4000, Liège, Belgium.
Nicole HoweMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, D02 R590, Ireland.
Chia-Ying HuangMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, D02 R590, Ireland.
Vincent OliericSwiss Light Source, Paul Scherrer Institute, CH-5232, Villigen, Switzerland.
Rangana WarshamanageSwiss Light Source, Paul Scherrer Institute, CH-5232, Villigen, Switzerland.
Thierry TouzéInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91190, Gif-sur-Yvette, Cedex, France.
Dietmar WeichertMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, D02 R590, Ireland.ORCID http://orcid.org/0000-0002-0694-7671
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Meitian WangSwiss Light Source, Paul Scherrer Institute, CH-5232, Villigen, Switzerland.
Fred KerffCentre d'Ingénierie des Protéines, InBioS, Université de Liège, allée du 6 Août 19, Bât B5a, 4000, Liège, Belgium.
Martin CaffreyMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, D02 R590, Ireland. martin.caffrey@tcd.ie.
Trinity College Dublin · IEPaul Scherrer Institute · CHUniversity of Liège · BEUniversité Paris-Sud · FRUniversity of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

As a protective envelope surrounding the bacterial cell, the peptidoglycan sacculus is a site of vulnerability and an antibiotic target. Peptidoglycan components, assembled in the cytoplasm, are shuttled across the membrane in a cycle that uses undecaprenyl-phosphate. A product of peptidoglycan synthesis, undecaprenyl-pyrophosphate, is converted to undecaprenyl-phosphate for reuse in the cycle by the membrane integral pyrophosphatase, BacA. To understand how BacA functions, we determine its crystal structure at 2.6 Å resolution. The enzyme is open to the periplasm and to the periplasmic leaflet via a pocket that extends into the membrane. Conserved residues map to the pocket where pyrophosphorolysis occurs. BacA incorporates an interdigitated inverted topology repeat, a topology type thus far only reported in transporters and channels. This unique topology raises issues regarding the ancestry of BacA, the possibility that BacA has alternate active sites on either side of the membrane and its possible function as a flippase.

Indexed as

Amino Acid SequenceCrystallography, X-RayEscherichia coli ProteinsModels, BiologicalMolecular Sequence DataPeptidoglycanPhosphoric Monoester HydrolasesPolyisoprenyl PhosphatesProtein Structure, SecondaryPyrophosphatasesBacA protein, E coliEscherichia coli ProteinsPeptidoglycanPhosphoric Monoester HydrolasesPolyisoprenyl PhosphatesPyrophosphatasesundecaprenyl pyrophosphateundecaprenyl pyrophosphate phosphatase

Identifiers

PMID29540682
PMCPMC5852022
OpenAlexW2792377336

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.