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7ZC1

Subtomogram averaging of Rubisco from Cyanobium carboxysome

Summary for 7ZC1
Entry DOI10.2210/pdb7zc1/pdb
EMDB information14589 14590 14592 14593 14617
DescriptorRibulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase, small subunit (2 entities in total)
Functional Keywordsrubisco, alpha carboxysomes, unknown function
Biological sourceCyanobium sp. PCC 7001
More
Total number of polymer chains16
Total formula weight523953.14
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 citationNi, 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: 35879301
DOI: 10.1038/s41467-022-32004-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

237735

数据于2025-06-18公开中

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