ArticleProtein science : a publication of the Protein Society2015
An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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.
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.
Who cites it
22 citing papers in PubMed.
- Drug resistance and tumor heterogeneity: cells and ensembles.Biophysical reviews · 2025Review
- Monatomic ions influence substrate permeation across bacterial microcompartment shells.Scientific reports · 2023Article
- Evolutionary relationships among shell proteins of carboxysomes and metabolosomes.Current opinion in microbiology · 2021Review
- Selective molecular transport across the protein shells of bacterial microcompartments.Current opinion in microbiology · 2021Review
- Recent structural insights into bacterial microcompartment shells.Current opinion in microbiology · 2021Review
- Variety of size and form of GRM2 bacterial microcompartment particles.Protein science : a publication of the Protein Society · 2021Article
- Advances in the World of Bacterial Microcompartments.Trends in biochemical sciences · 2021Review
- Genetically Encodable Scaffolds for Optimizing Enzyme Function.Molecules (Basel, Switzerland) · 2021Review
- MCPdb: The bacterial microcompartment database.PloS one · 2021Article
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.Nature communications · 2020Article
- Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment ofMicrobiology (Reading, England) · 2019Article
- Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme.Frontiers in bioengineering and biotechnology · 2019Article
- A Bacterial Microcompartment Is Used for Choline Fermentation by Escherichia coli 536.Journal of bacteriology · 2018Article
- Microfocus diffraction from different regions of a protein crystal: structural variations and unit-cell polymorphism.Acta crystallographica. Section D, Structural biology · 2018Article
- Bacterial microcompartments.Nature reviews. Microbiology · 2018Review
- Crystal structures of β-carboxysome shell protein CcmP: ligand binding correlates with the closed or open central pore.Journal of experimental botany · 2017Article
- The function of the PduJ microcompartment shell protein is determined by the genomic position of its encoding gene.Molecular microbiology · 2016Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Protein Science best paper awards to Tracy Clinton and Michael Thompson.Protein science : a publication of the Protein Society · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The ethanolamine utilization (Eut) microcompartment is a protein-based metabolic organelle that is strongly associated with pathogenesis in bacteria that inhabit the human gut. The exterior shell of this elaborate protein complex is composed from a few thousand copies of BMC-domain shell proteins, which form a semi-permeable diffusion barrier that provides the interior enzymes with substrates and cofactors while simultaneously retaining metabolic intermediates. The ability of this protein shell to regulate passage of substrate and cofactor molecules is critical for microcompartment function, but the details of how this diffusion barrier can allow the passage of large cofactors while still retaining small intermediates remain unclear. Previous work has revealed two conformations of the EutL shell protein, providing substantial evidence for a gated pore that might allow the passage of large cofactors. Here we report structural and biophysical evidence to show that ethanolamine, the substrate of the Eut microcompartment, acts as a negative allosteric regulator of EutL pore opening. Specifically, a series of X-ray crystal structures of EutL from Clostridium perfringens, along with equilibrium binding studies, reveal that ethanolamine binds to EutL at a site that exists in the closed-pore conformation and which is incompatible with opening of the large pore for cofactor transport. The allosteric mechanism we propose is consistent with the cofactor requirements of the Eut microcompartment, leading to a new model for EutL function. Furthermore, our results suggest the possibility of redox modulation of the allosteric mechanism, opening potentially new lines of investigation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.