8B12
cryo-EM structure of carboxysomal mini-shell: icosahedral assembly from CsoS4A/1A and CsoS2 co-expression (T = 9)
Summary for 8B12
| Entry DOI | 10.2210/pdb8b12/pdb |
| EMDB information | 15798 15799 15801 |
| Descriptor | Major carboxysome shell protein CsoS1A, Carboxysome shell vertex protein CsoS4A, Carboxysome assembly protein CsoS2B, ... (4 entities in total) |
| Functional Keywords | carboxysome, shell, icosahedral symmetry, structural protein |
| Biological source | Halothiobacillus neapolitanus More |
| Total number of polymer chains | 10 |
| Total formula weight | 180190.14 |
| Authors | |
| Primary citation | Ni, T.,Jiang, Q.,Ng, P.C.,Shen, J.,Dou, H.,Zhu, Y.,Radecke, J.,Dykes, G.F.,Huang, F.,Liu, L.N.,Zhang, P. Intrinsically disordered CsoS2 acts as a general molecular thread for alpha-carboxysome shell assembly. Nat Commun, 14:5512-5512, 2023 Cited by PubMed 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. PubMed: 37679318DOI: 10.1038/s41467-023-41211-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.86 Å) |
Structure validation
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