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TitleSingle-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome.
Journal, issue, pagesStructure, Vol. 31, Issue 6, Page 677-688.e4, Year 2023
Publish dateJun 1, 2023
AuthorsSasha L Evans / Monsour M J Al-Hazeem / Daniel Mann / Nicolas Smetacek / Andrew J Beavil / Yaqi Sun / Taiyu Chen / Gregory F Dykes / Lu-Ning Liu / Julien R C Bergeron /
PubMed AbstractCarboxysomes are proteinaceous bacterial microcompartments that sequester the key enzymes for carbon fixation in cyanobacteria and some proteobacteria. They consist of a virus-like icosahedral shell, ...Carboxysomes are proteinaceous bacterial microcompartments that sequester the key enzymes for carbon fixation in cyanobacteria and some proteobacteria. They consist of a virus-like icosahedral shell, encapsulating several enzymes, including ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO), responsible for the first step of the Calvin-Benson-Bassham cycle. Despite their significance in carbon fixation and great bioengineering potentials, the structural understanding of native carboxysomes is currently limited to low-resolution studies. Here, we report the characterization of a native α-carboxysome from a marine cyanobacterium by single-particle cryoelectron microscopy (cryo-EM). We have determined the structure of its RuBisCO enzyme, and obtained low-resolution maps of its icosahedral shell, and of its concentric interior organization. Using integrative modeling approaches, we have proposed a complete atomic model of an intact carboxysome, providing insight into its organization and assembly. This is critical for a better understanding of the carbon fixation mechanism and toward repurposing carboxysomes in synthetic biology for biotechnological applications.
External linksStructure / PubMed:37015227 / PubMed Central
MethodsEM (single particle)
Resolution2.87 - 20.0 Å
Structure data

EMDB-14376: Cryo-EM structure of the Cyanobium sp. PCC 7001 RuBisCO enzyme at 3.8 A resolution with C1 symmetry
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-14377: Cryo-EM structure of Cyanobium sp. PCC 7001 carboxysome shell
Method: EM (single particle) / Resolution: 18.25 Å

EMDB-14379: Cryo-EM structure of an intact carboxysome - core layer
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-14380: Cryo-EM structure of the Cyanobium sp. PCC 7001 Carboxysome internal density outer layer
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-14381: Cryo-EM structure of the Cyanobium sp. PCC 7001 Carboxysome internal density middle layer
Method: EM (single particle) / Resolution: 20.0 Å

14385

7yyo

EMDB-14385, PDB-7yyo:
Cryo-EM structure of an a-carboxysome RuBisCO enzyme at 2.9 A resolution
Method: EM (single particle) / Resolution: 2.87 Å

PDB-8cmy:
Structure of the Cyanobium sp. PCC 7001 determined with C1 symmetry
Method: ELECTRON MICROSCOPY / Resolution: 3.79 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CAP:
2-CARBOXYARABINITOL-1,5-DIPHOSPHATE

Source
  • Cyanobium sp. PCC 7001 (bacteria)
  • cyanobium (bacteria)
KeywordsPHOTOSYNTHESIS / Carboxysome / carbon fixation / cyanobacteria

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