7ZC1
Subtomogram averaging of Rubisco from Cyanobium carboxysome
Summary for 7ZC1
Entry DOI | 10.2210/pdb7zc1/pdb |
EMDB information | 14589 14590 14592 14593 14617 |
Descriptor | Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase, small subunit (2 entities in total) |
Functional Keywords | rubisco, alpha carboxysomes, unknown function |
Biological source | Cyanobium sp. PCC 7001 More |
Total number of polymer chains | 16 |
Total formula weight | 523953.14 |
Authors | Ni, T.,Zhu, Y.,Seaton-Burn, W.,Zhang, P. (deposition date: 2022-03-25, release date: 2022-07-06, Last modification date: 2024-07-24) |
Primary citation | Ni, T.,Sun, Y.,Burn, W.,Al-Hazeem, M.M.J.,Zhu, Y.,Yu, X.,Liu, L.N.,Zhang, P. Structure and assembly of cargo Rubisco in two native alpha-carboxysomes. Nat Commun, 13:4299-4299, 2022 Cited by PubMed Abstract: Carboxysomes are a family of bacterial microcompartments in cyanobacteria and chemoautotrophs. They encapsulate Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and carbonic anhydrase catalyzing carbon fixation inside a proteinaceous shell. How Rubisco complexes pack within the carboxysomes is unknown. Using cryo-electron tomography, we determine the distinct 3D organization of Rubisco inside two distant α-carboxysomes from a marine α-cyanobacterium Cyanobium sp. PCC 7001 where Rubiscos are organized in three concentric layers, and from a chemoautotrophic bacterium Halothiobacillus neapolitanus where they form intertwining spirals. We further resolve the structures of native Rubisco as well as its higher-order assembly at near-atomic resolutions by subtomogram averaging. The structures surprisingly reveal that the authentic intrinsically disordered linker protein CsoS2 interacts with Rubiscos in native carboxysomes but functions distinctively in the two α-carboxysomes. In contrast to the uniform Rubisco-CsoS2 association in the Cyanobium α-carboxysome, CsoS2 binds only to the Rubiscos close to the shell in the Halo α-carboxysome. Our findings provide critical knowledge of the assembly principles of α-carboxysomes, which may aid in the rational design and repurposing of carboxysome structures for new functions. PubMed: 35879301DOI: 10.1038/s41467-022-32004-w PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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