Evidence map›Paper›PMID 23528827›Full record

ArticleJournal of molecular biology2013

Structure of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ.

Christopher H S Aylett, Thierry Izoré, Linda A Amos, Jan Löwe

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. The Biology of Nucleus-Forming Jumbo Phages.Annual review of genetics · 2025
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  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Functional and evolutionary analysis of viral proteins containing a Rossmann-like fold.Protein science : a publication of the Protein Society · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Inside out: tubulin cytomotive filaments versus microtubules.Structure (London, England : 1993) · 2014
    Article
  20. 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

4 authors at 1 institution in 1 country.

Christopher H S AylettMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Thierry Izoré
Linda A Amos
Jan Löwe
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184313Medical Research Council MC_U105184326Medical Research Council U105184326
6 · The paper itself

Abstract

Pseudomonas ΦKZ-like bacteriophages encode a group of related tubulin/FtsZ-like proteins believed to be essential for the correct centring of replicated bacteriophage virions within the bacterial host. In this study, we present crystal structures of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ in both the monomeric and protofilament states, revealing that ΦKZ TubZ undergoes structural changes required to polymerise, forming a canonical tubulin/FtsZ-like protofilament. Combining our structures with previous work, we propose a polymerisation-depolymerisation cycle for the Pseudomonas bacteriophage subgroup of tubulin/FtsZ-like proteins. Electron cryo-microscopy of ΦKZ TubZ filaments polymerised in vitro implies a long-pitch helical arrangement for the constituent protofilaments. Intriguingly, this feature is shared by the other known subgroup of bacteriophage tubulin/FtsZ-like proteins from Clostridium species, which are thought to be involved in partitioning the genomes of bacteriophages adopting a pseudo-lysogenic life cycle.

Indexed as

Amino Acid SequenceCryoelectron MicroscopyCrystallography, X-RayModels, MolecularMolecular Sequence DataProtein MultimerizationPseudomonas PhagesSequence AlignmentViral ProteinsViral Proteins

Identifiers

PMID23528827
PMCPMC3678025
OpenAlexW2097210034

What OpenQuestion holds

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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.