ArticleProtein science : a publication of the Protein Society2013
Bacterial microcompartment shells of diverse functional types possess pentameric vertex proteins.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 74 citations in OpenAlex.
- Molecular basis of the biogenesis of a protein organelle for ethanolamine utilization.Science advances · 2025Article
- IntegrativemSystems · 2024Article
- A single shell protein plays a major role in choline transport across the shell of the choline utilization microcompartment ofMicrobiology (Reading, England) · 2023Article
- Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale.Advanced materials (Deerfield Beach, Fla.) · 2023Article
- Linking the Salmonella enterica 1,2-Propanediol Utilization Bacterial Microcompartment Shell to the Enzymatic Core via the Shell Protein PduB.Journal of bacteriology · 2022Article
- Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology.Nature communications · 2022Article
- Biogenesis of a bacterial metabolosome for propanediol utilization.Nature communications · 2022Article
- Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Recent structural insights into bacterial microcompartment shells.Current opinion in microbiology · 2021Review
- Selective molecular transport across the protein shells of bacterial microcompartments.Current opinion in microbiology · 2021Review
- Variety of size and form of GRM2 bacterial microcompartment particles.Protein science : a publication of the Protein Society · 2021Article
- Computational and Experimental Approaches to Controlling Bacterial Microcompartment Assembly.ACS central science · 2021Article
- Article
- MCPdb: The bacterial microcompartment database.PloS one · 2021Article
- Symmetry breaking and structural polymorphism in a bacterial microcompartment shell protein for choline utilization.Protein science : a publication of the Protein Society · 2020Article
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Decoding the stoichiometric composition and organisation of bacterial metabolosomes.Nature communications · 2020Article
- Genetic Characterization of a Glycyl Radical Microcompartment Used for 1,2-Propanediol Fermentation by Uropathogenic Escherichia coli CFT073.Journal of bacteriology · 2020Article
- Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.Nature communications · 2020Article
- Occurrence and stability of hetero-hexamer associations formed by β-carboxysome CcmK shell components.PloS one · 2019Article
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5 authors at 1 institution in 1 country.
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Abstract
Bacterial microcompartments (MCPs) are large proteinaceous structures comprised of a roughly icosahedral shell and a series of encapsulated enzymes. MCPs carrying out three different metabolic functions have been characterized in some detail, while gene expression and bioinformatics studies have implicated other types, including one believed to perform glycyl radical-based metabolism of 1,2-propanediol (Grp). Here we report the crystal structure of a protein (GrpN), which is presumed to be part of the shell of a Grp-type MCP in Rhodospirillum rubrum F11. GrpN is homologous to a family of proteins (EutN/PduN/CcmL/CsoS4) whose members have been implicated in forming the vertices of MCP shells. Consistent with that notion, the crystal structure of GrpN revealed a pentameric assembly. That observation revived an outstanding question about the oligomeric state of this protein family: pentameric forms (for CcmL and CsoS4A) and a hexameric form (for EutN) had both been observed in previous crystal structures. To clarify these confounding observations, we revisited the case of EutN. We developed a molecular biology-based method for accurately determining the number of subunits in homo-oligomeric proteins, and found unequivocally that EutN is a pentamer in solution. Based on these convergent findings, we propose the name bacterial microcompartment vertex for this special family of MCP shell proteins.
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