ArticleProtein science : a publication of the Protein Society2020
Symmetry breaking and structural polymorphism in a bacterial microcompartment shell protein for choline utilization.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A suite of designed protein cages using machine learning and protein fragment-based protocols.Structure (London, England : 1993) · 2024Article
- A Suite of Designed Protein Cages Using Machine Learning Algorithms and Protein Fragment-Based Protocols.bioRxiv : the preprint server for biology · 2023Article
- Computational Design of Single-Peptide Nanocages with Nanoparticle Templating.Molecules (Basel, Switzerland) · 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
- Advances in the World of Bacterial Microcompartments.Trends in biochemical sciences · 2021Review
- 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
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6 authors.
Funding
Abstract
Bacterial microcompartments are protein-based organelles that carry out specialized metabolic functions in diverse bacteria. Their outer shells are built from several thousand protein subunits. Some of the architectural principles of bacterial microcompartments have been articulated, with lateral packing of flat hexameric BMC proteins providing the basic foundation for assembly. Nonetheless, a complete understanding has been elusive, partly owing to polymorphic mechanisms of assembly exhibited by most microcompartment types. An earlier study of one homologous BMC shell protein subfamily, EutS/PduU, revealed a profoundly bent, rather than flat, hexameric structure. The possibility of a specialized architectural role was hypothesized, but artifactual effects of crystallization could not be ruled out. Here we report a series of crystal structures of an orthologous protein, CutR, from a glycyl-radical type choline-utilizing microcompartment from the bacterium Streptococcus intermedius. Depending on crystal form, expression construct, and minor mutations, a range of novel quaternary architectures was observed, including two spiral hexagonal assemblies. A new graphical approach helps illuminate the variations in BMC hexameric structure, with results substantiating the idea that the EutS/PduU/CutR subfamily of BMC proteins may endow microcompartment shells with flexible modes of assembly.
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