Evidence map›Paper›PMID 22659006›Full record

ArticleJournal of molecular biology2012

Filaments from Ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices.

Xiong Yu, Charles Goforth, Carolin Meyer, Reinhard Rachel, Reinhard Wirth, Gunnar F Schröder, Edward H Egelman

Abstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Cryo-EM of bacterial pili and archaeal flagellar filaments.Current opinion in structural biology · 2017
    Review
  7. Article
  8. Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Motility and Ultrastructure ofFrontiers in microbiology · 2016
    Article
  10. Review
  11. Article
  12. Editorial.FEMS microbiology reviews · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. 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

7 authors at 3 institutions in 2 countries.

Xiong YuDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA.
Charles Goforth
Carolin Meyer
Reinhard Rachel
Reinhard Wirth
Gunnar F Schröder
Edward H Egelman
University of Regensburg · DEUniversity of Virginia · USForschungszentrum Jülich · DE

Funding

TRAINING IN CELL AND MOLECULAR BIOLOGYT32GM008136 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI STUKENBERG, P. TODD · 1985 to 2020
$8.5M
Methods for the Analysis of Helical Macromolecular ComplexesR01EB001567 · NIBIB · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI EGELMAN, EDWARD H. · 2003 to 2014
$3.6M
NIBIB NIH HHS EB001567NIBIB NIH HHS R01 EB001567NIGMS NIH HHS T32 GM008136
6 · The paper itself

Abstract

Bacterial motility is driven by the rotation of flagellar filaments that supercoil. The supercoiling involves the switching of coiled-coil protofilaments between two different states. In archaea, the flagellar filaments responsible for motility are formed by proteins with distinct homology in their N-terminal portion to bacterial Type IV pilins. The bacterial pilins have a single N-terminal hydrophobic α-helix, not the coiled coil found in flagellin. We have used electron cryo-microscopy to study the adhesion filaments from the archaeon Ignicoccus hospitalis. While I. hospitalis is non-motile, these filaments make transitions between rigid stretches and curved regions and appear morphologically similar to true archaeal flagellar filaments. A resolution of ~7.5Å allows us to unambiguously build a model for the packing of these N-terminal α-helices, and this packing is different from several bacterial Type IV pili whose structure has been analyzed by electron microscopy and modeling. Our results show that the mechanism responsible for the supercoiling of bacterial flagellar filaments cannot apply to archaeal filaments.

Indexed as

Archaeal ProteinsCryoelectron MicroscopyDesulfurococcaceaeFimbriae ProteinsModels, MolecularProtein Structure, SecondaryArchaeal ProteinsFimbriae Proteins

Identifiers

PMID22659006
PMCPMC3599786
OpenAlexW1973985899

What OpenQuestion holds

Textmetadata
LicenceTDM
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.