The carbon fixation machinery α-carboxysome of the marine cyanobacterium Prochlorococcus is composed of an icosahedral-like proteinaceous shell that encapsulates the enzymes RuBisCO and carbonic anhydrase. Our cryo-EM structure reveals how thousands of protein components self-assemble into the α-carboxysome and characterizes the multivalent interactions by which the scaffolding protein CsoS2 crosslinks the shell with internal RuBisCO molecules.
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References
Badger, M. R. & Price, G. D. CO2 concentrating mechanisms in cyanobacteria: molecular components, their diversity and evolution. J. Exp. Bot. 54, 609–622 (2003). A review that presents the CO2-concentrating mechanism in cyanobacteria.
Kerfeld, C. A., Aussignargues, C., Zarzycki, J., Cai, F. & Sutter, M. Bacterial microcompartments. Nat. Rev. Microbiol. 16, 277–290 (2018). A review that presents the progress on the structures and functions of bacterial microcompartments.
Zhu, D. et al. Pushing the resolution limit by correcting the Ewald sphere effect in single-particle Cryo-EM reconstructions. Nat. Commun. 9, 1552 (2018). This paper elucidates the theory and application of block-based reconstruction in cryo-EM.
Oltrogge, L. M. et al. Multivalent interactions between CsoS2 and Rubisco mediate alpha-carboxysome formation. Nat. Struct. Mol. Biol. 27, 281–287 (2020). This paper reveals the interaction mode between the N-terminal motif of CsoS2 and RuBisCO.
Ni, T. et al. Intrinsically disordered CsoS2 acts as a general molecular thread for alpha-carboxysome shell assembly. Nat. Commun. 14, 5512 (2023). This paper elucidates the interaction pattern of C-terminal motifs of CsoS2 binding to the inner surface of the α-carboxysome shell.
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This is a summary of: Zhou, R. Q. et al. Structure and assembly of the α-carboxysome in the marine cyanobacterium Prochlorococcus. Nat. Plants https://doi.org/10.1038/s41477-024-01660-9 (2024).
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Structure of intact α-carboxysome specifies role of CsoS2 in shell assembly. Nat. Plants 10, 535–536 (2024). https://doi.org/10.1038/s41477-024-01667-2
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DOI: https://doi.org/10.1038/s41477-024-01667-2