Evidence map›Paper›PMID 31613220›Full record

ArticleeLife2019

Structural diversity of oligomeric β-propellers with different numbers of identical blades.

Evgenia Afanasieva, Indronil Chaudhuri, Jörg Martin, Eva Hertle, Astrid Ursinus, Vikram Alva, Marcus D Hartmann, Andrei N Lupas

Abstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Similar protein segments shared between domains of different evolutionary lineages.Protein science : a publication of the Protein Society · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The role of WDR76 protein in human diseases.Bosnian journal of basic medical sciences · 2021
    Review
  13. Article
  14. Development and applications of artificial symmetrical proteins.Computational and structural biotechnology journal · 2020
    Review
  15. 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

8 authors.

Evgenia Afanasieva *Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Indronil Chaudhuri *Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Jörg Martin *Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Eva HertleDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Astrid UrsinusDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Vikram AlvaDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0003-1188-473X
Marcus D HartmannDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0001-6937-5677
Andrei N LupasDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0002-1959-4836

Funding

Volkswagen Foundation Life Grant 94 810
6 · The paper itself

Abstract

β-Propellers arise through the amplification of a supersecondary structure element called a blade. This process produces toroids of between four and twelve repeats, which are almost always arranged sequentially in a single polypeptide chain. We found that new propellers evolve continuously by amplification from single blades. We therefore investigated whether such nascent propellers can fold as homo-oligomers before they have been fully amplified within a single chain. One- to six-bladed building blocks derived from two seven-bladed WD40 propellers yielded stable homo-oligomers with six to nine blades, depending on the size of the building block. High-resolution structures for tetramers of two blades, trimers of three blades, and dimers of four and five blades, respectively, show structurally diverse propellers and include a novel fold, highlighting the inherent flexibility of the WD40 blade. Our data support the hypothesis that subdomain-sized fragments can provide structural versatility in the evolution of new proteins.

Indexed as

Protein FoldingActinobacteriaBacterial ProteinsProtein ConformationProtein MultimerizationProtein Serine-Threonine KinasesBacterial ProteinsPkwA protein, Thermomonospora curvataProtein Serine-Threonine Kinasesbeta-propellersbiochemistrychemical biologymolecular biophysicsnoneoligomeric proteinsprotein designprotein evolutionsequence repeat amplificatistructural biology

Identifiers

PMID31613220
PMCPMC6805158

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Registered trials

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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.