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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond Krios II-Titan Krios II at Diamond Krios III-Titan Krios III at Diamond Krios IV-Titan Krios IV at Diamond	Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly Tao Ni , Qiuyao Jiang , Pei Cing Ng , Juan Shen , Hao Dou , Yanan Zhu , Julika Radecke , Gregory F. Dykes , Fang Huang , Lu-Ning Liu , Peijun Zhang Nature Communications 14 DOI: 10.1038/s41467-023-41211-y Diamond Proposal Number(s): [29812, 28713] Open Access Show Abstract ▼ Abstract: Carboxysomes are a paradigm of self-assembling proteinaceous organelles found in nature, offering compartmentalisation of enzymes and pathways to enhance carbon fixation. In α-carboxysomes, the disordered linker protein CsoS2 plays an essential role in carboxysome assembly and Rubisco encapsulation. Its mechanism of action, however, is not fully understood. Here we synthetically engineer α-carboxysome shells using minimal shell components and determine cryoEM structures of these to decipher the principle of shell assembly and encapsulation. The structures reveal that the intrinsically disordered CsoS2 C-terminus is well-structured and acts as a universal “molecular thread” stitching through multiple shell protein interfaces. We further uncover in CsoS2 a highly conserved repetitive key interaction motif, [IV]TG, which is critical to the shell assembly and architecture. Our study provides a general mechanism for the CsoS2-governed carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications.	Sep 2023

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Krios I-Titan Krios I at Diamond
Krios II-Titan Krios II at Diamond
Krios III-Titan Krios III at Diamond
Krios IV-Titan Krios IV at Diamond

Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly