Evidence map›Paper›PMID 31959751›Full record

ArticleNature communications2020

Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.

Gints Kalnins, Eva-Emilija Cesle, Juris Jansons, Janis Liepins, Anatolij Filimonenko, Kaspars Tars

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  5. Atomic view of photosynthetic metabolite permeability pathways and confinement in synthetic carboxysome shells.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  8. IntegrativemSystems · 2024
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  11. Functionalization of bacterial microcompartment shell interior with cysteine containing peptides enhances the iron and cobalt loading capacity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
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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

6 authors at 3 institutions in 2 countries.

Gints KalninsLatvian Biomedical Research and Study Centre, Ratsupites 1, Riga, 1067, Latvia. gints@biomed.lu.lv.ORCID http://orcid.org/0000-0002-9593-6308
Eva-Emilija CesleLatvian Biomedical Research and Study Centre, Ratsupites 1, Riga, 1067, Latvia.
Juris JansonsLatvian Biomedical Research and Study Centre, Ratsupites 1, Riga, 1067, Latvia.
Janis LiepinsInstitute of Microbiology and Biotechnology, University of Latvia, Jelgavas 1, Riga, 1004, Latvia.ORCID http://orcid.org/0000-0001-7778-5561
Anatolij FilimonenkoCentral European Institute of Technology, Masaryk University, Kamenice 753/5, 62500, Brno, Czech Republic.
Kaspars TarsLatvian Biomedical Research and Study Centre, Ratsupites 1, Riga, 1067, Latvia.
Latvian Biomedical Research and Study Centre · LVCentral European Institute of Technology · CZUniversity of Latvia · LV

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial microcompartments (BMCs) are prokaryotic organelles consisting of a protein shell and an encapsulated enzymatic core. BMCs are involved in several biochemical processes, such as choline, glycerol and ethanolamine degradation and carbon fixation. Since non-native enzymes can also be encapsulated in BMCs, an improved understanding of BMC shell assembly and encapsulation processes could be useful for synthetic biology applications. Here we report the isolation and recombinant expression of BMC structural genes from the Klebsiella pneumoniae GRM2 locus, the investigation of mechanisms behind encapsulation of the core enzymes, and the characterization of shell particles by cryo-EM. We conclude that the enzymatic core is encapsulated in a hierarchical manner and that the CutC choline lyase may play a secondary role as an adaptor protein. We also present a cryo-EM structure of a pT = 4 quasi-symmetric icosahedral shell particle at 3.3 Å resolution, and demonstrate variability among the minor shell forms.

Indexed as

Bacterial ProteinsCholineCryoelectron MicroscopyGenetic LociKlebsiella pneumoniaeLyasesOrganellesRecombinant ProteinsSynthetic BiologyBacterial ProteinsCholineLyasesRecombinant Proteins

Identifiers

PMID31959751
PMCPMC6971018
OpenAlexW3000649071

What OpenQuestion holds

Textmetadata
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.