Evidence map›Paper›PMID 26665178›Full record

ArticleScience advances2015

Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.

Chaowei Shi, Pascal Fricke, Lin Lin, Veniamin Chevelkov, Melanie Wegstroth, Karin Giller, Stefan Becker, Martin Thanbichler, Adam Lange

Abstract read
In one paragraph

Article in Science advances, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
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  3. Article
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  6. Article
  7. Article
  8. Halofilins as emerging bactofilin families of archaeal cell shape plasticity orchestrators.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. VirB, a key transcriptional regulator ofbioRxiv : the preprint server for biology · 2023
    Article
  12. Article
  13. Hydrogen Isotope Separation Using a Metal-Organic Cage Built from Macrocycles.Angewandte Chemie (International ed. in English) · 2022
    Article
  14. Article
  15. Chemical reviews · 2022
    Review
  16. Article
  17. Article
  18. Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensionalProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021
    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

9 authors.

Chaowei ShiDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
Pascal FrickeDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
Lin LinProkaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany. ; Faculty of Biology, Philipps-Universität, 35043 Marburg, Germany.
Veniamin ChevelkovDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
Melanie WegstrothDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.ORCID 0000-0002-3249-3917
Karin GillerDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.ORCID 0000-0002-4149-7899
Stefan BeckerDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Martin ThanbichlerProkaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany. ; Faculty of Biology, Philipps-Universität, 35043 Marburg, Germany. ; LOEWE Center for Synthetic Microbiology, Philipps-Universität, 35043 Marburg, Germany.
Adam LangeDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany. ; Institut für Biologie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bactofilins are a recently discovered class of cytoskeletal proteins of which no atomic-resolution structure has been reported thus far. The bacterial cytoskeleton plays an essential role in a wide range of processes, including morphogenesis, cell division, and motility. Among the cytoskeletal proteins, the bactofilins are bacteria-specific and do not have a eukaryotic counterpart. The bactofilin BacA of the species Caulobacter crescentus is not amenable to study by x-ray crystallography or solution nuclear magnetic resonance (NMR) because of its inherent noncrystallinity and insolubility. We present the atomic structure of BacA calculated from solid-state NMR-derived distance restraints. We show that the core domain of BacA forms a right-handed β helix with six windings and a triangular hydrophobic core. The BacA structure was determined to 1.0 Å precision (heavy-atom root mean square deviation) on the basis of unambiguous restraints derived from four-dimensional (4D) HN-HN and 2D C-C NMR spectra.

Indexed as

BactofilinsCytoskeletal proteinsProtein StructureSolid-state NMR

Identifiers

PMID26665178
PMCPMC4672760

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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.