{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ferlez BH"],"funding":["National Institute of Allergy and Infectious Diseases","U.S. Department of Energy","NIAID NIH HHS","Basic Energy Sciences","National Institutes of Health","Office of Science","NIH HHS"],"pagination":["e2212065"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10330516"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35(23)"],"pubmed_abstract":["Many bacteria use protein-based organelles known as bacterial microcompartments (BMCs) to organize and sequester sequential enzymatic reactions. Regardless of their specialized metabolic function, all BMCs are delimited by a shell made of multiple structurally redundant, yet functionally diverse, hexameric (BMC-H), pseudohexameric/trimeric (BMC-T), or pentameric (BMC-P) shell protein paralogs. When expressed without their native cargo, shell proteins have been shown to self-assemble into 2D sheets, open-ended nanotubes, and closed shells of ≈40 nm diameter that are being developed as scaffolds and nanocontainers for applications in biotechnology. Here, by leveraging a strategy for affinity-based purification, it is demonstrated that a wide range of empty synthetic shells, many differing in end-cap structures, can be derived from a glycyl radical enzyme-associated microcompartment. The range of pleomorphic shells observed, which span ≈2 orders of magnitude in size from ≈25 nm to ≈1.8 µm, reveal the remarkable plasticity of BMC-based biomaterials. In addition, new capped nanotube and nanocone morphologies are observed that are consistent with a multicomponent geometric model in which architectural principles are shared among asymmetric carbon, viral protein, and BMC-based structures."],"journal":["Advanced materials (Deerfield Beach, Fla.)"],"pubmed_title":["Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale."],"pmcid":["PMC10330516"],"funding_grant_id":["DE‐SC0023395","R01 AI114975","1R01AI114975‐06"],"pubmed_authors":["Kirst H","Nogales E","Kerfeld CA","Sutter M","Greber BJ","Ferlez BH"],"additional_accession":[]},"is_claimable":false,"name":"Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale.","description":"Many bacteria use protein-based organelles known as bacterial microcompartments (BMCs) to organize and sequester sequential enzymatic reactions. Regardless of their specialized metabolic function, all BMCs are delimited by a shell made of multiple structurally redundant, yet functionally diverse, hexameric (BMC-H), pseudohexameric/trimeric (BMC-T), or pentameric (BMC-P) shell protein paralogs. When expressed without their native cargo, shell proteins have been shown to self-assemble into 2D sheets, open-ended nanotubes, and closed shells of ≈40 nm diameter that are being developed as scaffolds and nanocontainers for applications in biotechnology. Here, by leveraging a strategy for affinity-based purification, it is demonstrated that a wide range of empty synthetic shells, many differing in end-cap structures, can be derived from a glycyl radical enzyme-associated microcompartment. The range of pleomorphic shells observed, which span ≈2 orders of magnitude in size from ≈25 nm to ≈1.8 µm, reveal the remarkable plasticity of BMC-based biomaterials. In addition, new capped nanotube and nanocone morphologies are observed that are consistent with a multicomponent geometric model in which architectural principles are shared among asymmetric carbon, viral protein, and BMC-based structures.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-06-02T08:38:30.148Z","creation":"2026-05-25T03:06:40.465Z"},"accession":"S-EPMC10330516","cross_references":{"pubmed":["36932732"],"doi":["10.1002/adma.202212065"]}}