Bacterial microcompartments are large supramolecular assemblies, resembling viruses in size and shape, found inside many bacterial cells. A protein-based shell encapsulates a series of sequentially acting enzymes in order to sequester certain sensitive metabolic processes within the cell. Crystal structures of the individual shell proteins have revealed details about how they self-assemble and how pores through their centers facilitate molecular transport into and out of the microcompartments. Biochemical and genetic studies have shown that enzymes are directed to the interior in some cases by special targeting sequences in their termini. Together, these findings open up prospects for engineering bacterial microcompartments with novel functionalities for applications ranging from metabolic engineering to targeted drug delivery.
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