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| Hauptseite > Publikationsdatenbank > Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome > print |
| Hauptseite > Publikationsdatenbank > Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome > print |
| 001 | 1006587 | ||
| 005 | 20250203103429.0 | ||
| 024 | 7 | _ | |a 10.1016/j.str.2023.03.008 |2 doi |
| 024 | 7 | _ | |a 0969-2126 |2 ISSN |
| 024 | 7 | _ | |a 1878-4186 |2 ISSN |
| 024 | 7 | _ | |a 10.34734/FZJ-2023-01728 |2 datacite_doi |
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| 100 | 1 | _ | |a Evans, Sasha L. |b 0 |
| 245 | _ | _ | |a Single-particle cryo-EM analysis of the shell architecture and internal organization of an intact α-carboxysome |
| 260 | _ | _ | |a Cambridge, Mass. |c 2023 |b Cell Press |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a 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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| 700 | 1 | _ | |a Al-Hazeem, Monsour M. J. |b 1 |
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| 700 | 1 | _ | |a Smetacek, Nicolas |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Beavil, Andrew J. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Sun, Yaqi |b 5 |
| 700 | 1 | _ | |a Chen, Taiyu |b 6 |
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| 700 | 1 | _ | |a Liu, Lu-Ning |0 P:(DE-Juel1)176583 |b 8 |e Corresponding author |
| 700 | 1 | _ | |a Bergeron, Julien R. C. |0 0000-0002-2841-9511 |b 9 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.str.2023.03.008 |g p. S0969212623000849 |0 PERI:(DE-600)2031189-8 |p S0969212623000849 |t Structure |v 31 |y 2023 |x 0969-2126 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/1006587/files/1-s2.0-S0969212623000849-main.pdf |y OpenAccess |
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