TY  - JOUR
AU  - Evans, Sasha L.
AU  - Al-Hazeem, Monsour M. J.
AU  - Mann, Daniel
AU  - Smetacek, Nicolas
AU  - Beavil, Andrew J.
AU  - Sun, Yaqi
AU  - Chen, Taiyu
AU  - Dykes, Gregory F.
AU  - Liu, Lu-Ning
AU  - Bergeron, Julien R. C.
TI  - Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome
JO  - Structure
VL  - 31
SN  - 0969-2126
CY  - Cambridge, Mass.
PB  - Cell Press
M1  - FZJ-2023-01728
SP  - S0969212623000849
PY  - 2023
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 37015227
UR  - <Go to ISI:>//WOS:001012177900001
DO  - DOI:10.1016/j.str.2023.03.008
UR  - https://juser.fz-juelich.de/record/1006587
ER  -