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| Hauptseite > Publikationsdatenbank > Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome |
| Hauptseite > Publikationsdatenbank > Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome |
| Journal Article | FZJ-2023-01728 |
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2023
Cell Press
Cambridge, Mass.
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Please use a persistent id in citations: doi:10.1016/j.str.2023.03.008 doi:10.34734/FZJ-2023-01728
Abstract: 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.
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