Evidence map›Paper›PMID 31822696›Full record

ArticleScientific reports2019

Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ.

Sarah C Lee, Richard Collins, Yu-Pin Lin, Mohammed Jamshad, Claire Broughton, Sarah A Harris, Benjamin S Hanson, Cecilia Tognoloni, Rosemary A Parslow, Ann E Terry and 6 more

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Biological insights from SMA-extracted proteins.Biochemical Society transactions · 2021
    Review
  6. Article
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

16 authors.

Sarah C LeeSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. S.lee.5@bham.ac.uk.
Richard CollinsFaculty of Life Sciences, A4032 Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK.
Yu-Pin LinSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
Mohammed JamshadSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
Claire BroughtonSchool of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.
Sarah A HarrisSchool of Physics and Astronomy and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.
Benjamin S HansonSchool of Physics and Astronomy and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.
Cecilia TognoloniDepartment of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.
Rosemary A ParslowSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
Ann E TerryMAX IV Laboratory Lund University, P.O. Box 118, SE-221 00, Lund, Sweden.
Alison RodgerDepartment of Molecular Sciences, Macquarie University, Macquarie, NSW, 2109, Australia.
Corinne J SmithSchool of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0003-3364-7946
Karen J EdlerDepartment of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.ORCID http://orcid.org/0000-0001-5822-0127
Robert FordFaculty of Life Sciences, A4032 Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK.
David I RoperSchool of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0003-0009-621X
Timothy R DaffornSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. T.R.Dafforn@bham.ac.uk.

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/J017310/1
6 · The paper itself

Abstract

The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. Direct binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray and neutron scattering, we determine the encapsulated-ZipA structure in isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three regions can be identified from the structure which correspond to, SMALP encapsulated membrane and ZipA transmembrane helix, a separate short compact tether, and ZipA globular head which binds FtsZ. The complex extends 12 nm from the membrane in a compact structure, supported by mesoscale modelling techniques, measuring the movement and stiffness of the regions within ZipA provides molecular scale analysis and visualisation of the early divisome.

Indexed as

Bacterial ProteinsCarrier ProteinsCell Cycle ProteinsCell DivisionCryoelectron MicroscopyCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsMembrane ProteinsProtein BindingBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaMembrane ProteinsZipA protein, E coli

Identifiers

PMID31822696
PMCPMC6904479

What OpenQuestion holds

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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.