Evidence map›Paper›PMID 30901520›Full record

ArticleACS synthetic biology2019

Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of Forming Icosahedral Shell Assemblies.

Markus Sutter, Sean McGuire, Bryan Ferlez, Cheryl A Kerfeld

Open access · greenAbstract read
In one paragraph

Article in ACS synthetic biology, 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
1.6field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Chemical reviews · 2026
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  10. Toward a glycyl radical enzyme containing synthetic bacterial microcompartment to produce pyruvate from formate and acetate.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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

4 authors at 2 institutions in 1 country.

Markus SutterEnvironmental Genomics and Systems Biology and Molecular Biophysics and Integrative Bioimaging Divisions , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.
Sean McGuireMSU-DOE Plant Research Laboratory , Michigan State University , East Lansing , Michigan 48824 , United States.
Bryan FerlezMSU-DOE Plant Research Laboratory , Michigan State University , East Lansing , Michigan 48824 , United States.ORCID 0000-0003-0505-2099
Cheryl A KerfeldEnvironmental Genomics and Systems Biology and Molecular Biophysics and Integrative Bioimaging Divisions , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , United States.ORCID 0000-0002-9977-8482
Lawrence Berkeley National Laboratory · USMichigan State University · US

Funding

Structure and Function of Bacterial Microcompartment Shells from Human PathogensR01AI114975 · NIAID · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI KERFELD, CHERYL A · 2015 to 2022
$3.0M
NIAID NIH HHS R01 AI114975
6 · The paper itself

Abstract

Bacterial microcompartments are subcellular compartments found in many prokaryotes; they consist of a protein shell that encapsulates enzymes that perform a variety of functions. The shell protects the cell from potentially toxic intermediates and colocalizes enzymes for higher efficiency. Accordingly, it is of considerable interest for biotechnological applications. We have previously structurally characterized an intact 40 nm shell comprising three different types of proteins. One of those proteins, BMC-H, forms a cyclic hexamer; here we have engineered a synthetic protein that consists of a tandem duplication of BMC-H connected by a short linker. The synthetic protein forms cyclic trimers that self-assemble to form a smaller (25 nm) icosahedral shell with gaps at the pentamer positions. When coexpressed in vivo with the pentamer fused to an affinity tag we can purify complete icosahedral shells. This engineered shell protein constitutes a minimal shell system to study permeability; reducing symmetry from 6- to 3-fold will allow for finer control of the pore environment. We have determined a crystal structure of this shell to guide rational engineering of this microcompartment shell for biotechnological applications.

Indexed as

BacteriaBacterial ProteinsCrystallography, X-RayProtein DomainsProtein EngineeringBacterial Proteinsbacterial microcompartmentprotein engineeringsynthetic biology

Identifiers

PMID30901520
PMCPMC6884138
OpenAlexW2924373035

What OpenQuestion holds

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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.