Many bacteria have primitive proteinaceous organelles that are known as bacterial microcompartments (BMCs). All BMCs share a common architecture, with a selectively permeable protein shell that encapsulates different metabolic enzymes. Although detailed structural information is available for the single components of the shell, how the shell assembles was unknown. In a new study, Sutter et al. determined the crystal structure of an intact shell from Haliangium ochraceum, thereby revealing the basic principles of its assembly. In particular, by using a recombinant system that contained selected components of the shell, the authors generated a complete 40 nm shell with a molecular mass of 6.5 MDa and determined its structure to a resolution of 3.5 Å. Considering that these structures are widely conserved in bacteria, these findings probably apply to various functionally distinct bacterial organelles.
References
Sutter, M. et al. Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell. Science 356, 1293–1297 (2017)
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Vacca, I. Insights into bacterial microcompartments. Nat Rev Microbiol 15, 451 (2017). https://doi.org/10.1038/nrmicro.2017.84
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DOI: https://doi.org/10.1038/nrmicro.2017.84