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8YVE

cryo-EM structure of carboxysomal midi-shell: icosahedral assembly from CsoS4A/4B/1A/1B/1C/1D and CsoS2 C-terminal co-expression (T = 9)

Summary for 8YVE
Entry DOI10.2210/pdb8yve/pdb
EMDB information39598
DescriptorMajor carboxysome shell protein CsoS1A, Carboxysome assembly protein CsoS2B, Carboxysome shell vertex protein CsoS4A (3 entities in total)
Functional Keywordscarboxysome, shell, icosahedron, structural protein
Biological sourceHalothiobacillus neapolitanus
More
Total number of polymer chains10
Total formula weight118046.54
Authors
Primary citationWang, P.,Li, J.,Li, T.,Li, K.,Ng, P.C.,Wang, S.,Chriscoli, V.,Basle, A.,Marles-Wright, J.,Zhang, Y.Z.,Liu, L.N.
Molecular principles of the assembly and construction of a carboxysome shell.
Sci Adv, 10:eadr4227-eadr4227, 2024
Cited by
PubMed Abstract: Intracellular compartmentalization enhances biological reactions, crucial for cellular function and survival. An example is the carboxysome, a bacterial microcompartment for CO fixation. The carboxysome uses a polyhedral protein shell made of hexamers, pentamers, and trimers to encapsulate Rubisco, increasing CO levels near Rubisco to enhance carboxylation. Despite their role in the global carbon cycle, the molecular mechanisms behind carboxysome shell assembly remain unclear. Here, we present a structural characterization of α-carboxysome shells generated from recombinant systems, which contain all shell proteins and the scaffolding protein CsoS2. Atomic-resolution cryo-electron microscopy of the shell assemblies, with a maximal size of 54 nm, unveil diverse assembly interfaces between shell proteins, detailed interactions of CsoS2 with shell proteins to drive shell assembly, and the formation of heterohexamers and heteropentamers by different shell protein paralogs, facilitating the assembly of larger empty shells. Our findings provide mechanistic insights into the construction principles of α-carboxysome shells and the role of CsoS2 in governing α-carboxysome assembly and functionality.
PubMed: 39612341
DOI: 10.1126/sciadv.adr4227
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.3 Å)
Structure validation

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