Two decades of structural and functional studies have revealed functions, structures and diversity of bacterial microcompartments. The protein-based organelles encapsulate diverse metabolic pathways in semipermeable, icosahedral or pseudo-icosahedral shells. One of the first discovered and characterized microcompartments are those involved in ethanolamine degradation. This review will summarize their function and assembly along with shared and unique characteristics with other microcompartment types. The modularity and self-assembling properties of their shell proteins make them valuable targets for bioengineering. Advances and prospects for shell protein engineering in vivo and in vitro for synthetic biology and biotechnology applications will be discussed.
Bibliographical noteFunding Information:
Research on the development of self-assembling protein materials in the Schmidt-Dannert Laboratory have been supported by Defense Threat Reduction Agency Grant HDTRA-15-0004 , Defense Advanced Research Projects Agency Contract HR0011-17-0038 , National Science Foundation Grant CBET-1916030 , MnDRIVE and the University of Minnesota’s Biocatalysis Initiative .
© 2021 Elsevier Ltd