ArticleThe Journal of biological chemistry2017
A Complete Structural Inventory of the Mycobacterial Microcompartment Shell Proteins Constrains Models of Global Architecture and Transport.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- A Generative Neuro-Symbolic AI for Protein Sequence Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Controlling nanocage assembly, towards developing a one-health "plug & play" platform for targeted therapy.Chemical communications (Cambridge, England) · 2025Review
- Comparative Pore Structure and Dynamics for Bacterial Microcompartment Shell Protein Assemblies in Sheets or Shells.ACS omega · 2024Article
- α-Carboxysome Size Is Controlled by the Disordered Scaffold Protein CsoS2.Biochemistry · 2024Article
- Assessment of oligomerization of bacterial micro-compartment shell components with the tripartite GFP reporter technology.PloS one · 2023Article
- Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology.Nature communications · 2022Article
- Evolutionary relationships among shell proteins of carboxysomes and metabolosomes.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
- Symmetry breaking and structural polymorphism in a bacterial microcompartment shell protein for choline utilization.Protein science : a publication of the Protein Society · 2020Article
- Bacterial microcompartments: catalysis-enhancing metabolic modules for next generation metabolic and biomedical engineering.BMC biology · 2019Review
- The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly.Structure (London, England : 1993) · 2019Article
- Heterohexamers Formed by CcmK3 and CcmK4 Increase the Complexity of Beta Carboxysome Shells.Plant physiology · 2019Article
- Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme.Frontiers in bioengineering and biotechnology · 2019Article
- Occurrence and stability of hetero-hexamer associations formed by β-carboxysome CcmK shell components.PloS one · 2019Article
- Comparative Genomic Analysis Reveals Novel Microcompartment-Associated Metabolic Pathways in the Human Gut Microbiome.Frontiers in genetics · 2019Article
- Structural and kinetic characterization of (The Journal of biological chemistry · 2018Article
- Bacterial microcompartments.Nature reviews. Microbiology · 2018Review
- Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell.Science (New York, N.Y.) · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial microcompartments are bacterial analogs of eukaryotic organelles in that they spatially segregate aspects of cellular metabolism, but they do so by building not a lipid membrane but a thin polyhedral protein shell. Although multiple shell protein structures are known for several microcompartment types, additional uncharacterized components complicate systematic investigations of shell architecture. We report here the structures of all four proteins proposed to form the shell of an uncharacterized microcompartment designated the Rhodococcus and Mycobacterium microcompartment (RMM), which, along with crystal interactions and docking studies, suggests possible models for the particle's vertex and edge organization. MSM0272 is a typical hexameric β-sandwich shell protein thought to form the bulk of the facet. MSM0273 is a pentameric β-barrel shell protein that likely plugs the vertex of the particle. MSM0271 is an unusual double-ringed bacterial microcompartment shell protein whose rings are organized in an offset position relative to all known related proteins. MSM0275 is related to MSM0271 but self-organizes as linear strips that may line the facet edge; here, the presence of a novel extendable loop may help ameliorate poor packing geometry of the rigid main particle at the angled edges. In contrast to previously characterized homologs, both of these proteins show closed pores at both ends. This suggests a model where key interactions at the vertex and edges are mediated at the inner layer of the shell by MSM0271 (encircling MSM0273) and MSM0275, and the facet is built from MSM0272 hexamers tiling in the outer layer of the shell.
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