%0 Journal Article
%A Evans, Sasha L.
%A Al-Hazeem, Monsour M. J.
%A Mann, Daniel
%A Smetacek, Nicolas
%A Beavil, Andrew J.
%A Sun, Yaqi
%A Chen, Taiyu
%A Dykes, Gregory F.
%A Liu, Lu-Ning
%A Bergeron, Julien R. C.
%T Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome
%J Structure
%V 31
%@ 0969-2126
%C Cambridge, Mass.
%I Cell Press
%M FZJ-2023-01728
%P S0969212623000849
%D 2023
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ 37015227
%U <Go to ISI:>//WOS:001012177900001
%R 10.1016/j.str.2023.03.008
%U https://juser.fz-juelich.de/record/1006587