Evidence map›Paper›PMID 27391173›Full record

ArticleProtein science : a publication of the Protein Society2017

Structure of the magnetosome-associated actin-like MamK filament at subnanometer resolution.

Julien R C Bergeron, Rachel Hutto, Ertan Ozyamak, Nancy Hom, Jesse Hansen, Olga Draper, Meghan E Byrne, Sepehr Keyhani, Arash Komeili, Justin M Kollman

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. A family of bacterial actin homologs forms a three-stranded tubular structure.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. X-ray and cryo-EM structures of monomeric and filamentous actin-like protein MamK reveal changes associated with polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. 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

10 authors.

Julien R C BergeronDepartment of Biochemistry, University of Washington, Seattle, Washington.
Rachel HuttoDepartment of Biochemistry, University of Washington, Seattle, Washington.
Ertan OzyamakDepartment of Plant and Microbial Biology, University of California, Berkeley, California.
Nancy HomDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington.
Jesse HansenDepartment of Biochemistry, University of British Columbia, Vancouver, British Columbia.
Olga DraperDepartment of Plant and Microbial Biology, University of California, Berkeley, California.
Meghan E ByrneDepartment of Plant and Microbial Biology, University of California, Berkeley, California.
Sepehr KeyhaniDepartment of Plant and Microbial Biology, University of California, Berkeley, California.
Arash KomeiliDepartment of Plant and Microbial Biology, University of California, Berkeley, California.
Justin M KollmanDepartment of Biochemistry, University of Washington, Seattle, Washington.

Funding

Molecular Mechanisms of Organelle Assembly by the Prokaryotic Actin Homolog MamKR01GM084122 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KOMEILI, ARASH · 2009 to 2017
$2.8M
NIGMS NIH HHS R01 GM084122
6 · The paper itself

Abstract

Magnetotactic bacteria possess cellular compartments called magnetosomes that sense magnetic fields. Alignment of magnetosomes in the bacterial cell is necessary for their function, and this is achieved through anchoring of magnetosomes to filaments composed of the protein MamK. MamK is an actin homolog that polymerizes upon ATP binding. Here, we report the structure of the MamK filament at ∼6.5 Å, obtained by cryo-Electron Microscopy. This structure confirms our previously reported double-stranded, nonstaggered architecture, and reveals the molecular basis for filament formation. While MamK is closest in sequence to the bacterial actin MreB, the longitudinal contacts along each MamK strand most closely resemble those of eukaryotic actin. In contrast, the cross-strand interface, with a surprisingly limited set of contacts, is novel among actin homologs and gives rise to the nonstaggered architecture.

Indexed as

Bacterial ProteinsMagnetosomesMagnetospirillumMultiprotein ComplexesBacterial ProteinsMultiprotein ComplexesactinCryo-EMfilamentsmagnetosome

Identifiers

PMID27391173
PMCPMC5192964

What OpenQuestion holds

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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.