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| Main Authors: | , , , , , |
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| Format: | Artículo científico |
| Language: | en |
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Proceedings of the National Academy of Sciences of the United States of America
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41223214/ |
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| _version_ | 1868266127737487361 |
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| author | Ng, Pei Cing Adegbite, Oluwatobi Li, Tianpei Baslé, Arnaud Marles-Wright, Jon Liu, Lu-Ning |
| author_facet | Ng, Pei Cing Adegbite, Oluwatobi Li, Tianpei Baslé, Arnaud Marles-Wright, Jon Liu, Lu-Ning Ng, Pei Cing Adegbite, Oluwatobi Li, Tianpei Baslé, Arnaud Marles-Wright, Jon Liu, Lu-Ning |
| collection | PubMed - marine biology |
| contents | Structure and encapsulation of carbonic anhydrase within the α-carboxysome. Ng, Pei Cing Adegbite, Oluwatobi Li, Tianpei Baslé, Arnaud Marles-Wright, Jon Liu, Lu-Ning Carbonic Anhydrases Ribulose-Bisphosphate Carboxylase Carbon Dioxide Halothiobacillus Bacterial Proteins Protein Multimerization Carbon Cycle Cryoelectron Microscopy Microscopy, Electron, Transmission Carboxysomes in cyanobacteria and certain proteobacteria enable efficient CO fixation by encapsulating ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and carbonic anhydrase (CA) within a semipermeable shell. Sequestered CA catalyze the rapid interconversion of CO and HCO, supplying elevated levels of CO to boost Rubisco carboxylation. Despite its essential role, the structure and encapsulation of CA within carboxysomes remain poorly understood. Here, we determined the molecular structure of α-carboxysomal CA from the model chemoautotrophic bacterium (CsoSCA). CsoSCA adopts a trimer-of-dimers oligomeric structure without the incorporation of a zinc ion at its symmetric center. Using synthetic minishells, we demonstrate that CsoSCA interacts with the CsoS1A shell hexamer and is incorporated into the minishells at the inner surface, independent of the CsoS2 linker protein. CsoSCA truncations suggest nonspecific interactions between CsoSCA and CsoS1A. We further show that CsoSCA bridges Rubisco and the shell facets. Our study offers insights into the assembly and encapsulation mechanisms of α-carboxysomes and provides the framework for reprogramming carboxysome structures for synthetic biology and biotechnological applications. |
| format | Artículo científico |
| id | pubmed_41223214 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Proceedings of the National Academy of Sciences of the United States of America |
| record_format | pubmed |
| spellingShingle | Structure and encapsulation of carbonic anhydrase within the α-carboxysome. Ng, Pei Cing Adegbite, Oluwatobi Li, Tianpei Baslé, Arnaud Marles-Wright, Jon Liu, Lu-Ning Carbonic Anhydrases Ribulose-Bisphosphate Carboxylase Carbon Dioxide Halothiobacillus Bacterial Proteins Protein Multimerization Carbon Cycle Cryoelectron Microscopy Microscopy, Electron, Transmission Structure and encapsulation of carbonic anhydrase within the α-carboxysome. Ng, Pei Cing Adegbite, Oluwatobi Li, Tianpei Baslé, Arnaud Marles-Wright, Jon Liu, Lu-Ning Carbonic Anhydrases Ribulose-Bisphosphate Carboxylase Carbon Dioxide Halothiobacillus Bacterial Proteins Protein Multimerization Carbon Cycle Cryoelectron Microscopy Microscopy, Electron, Transmission Carboxysomes in cyanobacteria and certain proteobacteria enable efficient CO fixation by encapsulating ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and carbonic anhydrase (CA) within a semipermeable shell. Sequestered CA catalyze the rapid interconversion of CO and HCO, supplying elevated levels of CO to boost Rubisco carboxylation. Despite its essential role, the structure and encapsulation of CA within carboxysomes remain poorly understood. Here, we determined the molecular structure of α-carboxysomal CA from the model chemoautotrophic bacterium (CsoSCA). CsoSCA adopts a trimer-of-dimers oligomeric structure without the incorporation of a zinc ion at its symmetric center. Using synthetic minishells, we demonstrate that CsoSCA interacts with the CsoS1A shell hexamer and is incorporated into the minishells at the inner surface, independent of the CsoS2 linker protein. CsoSCA truncations suggest nonspecific interactions between CsoSCA and CsoS1A. We further show that CsoSCA bridges Rubisco and the shell facets. Our study offers insights into the assembly and encapsulation mechanisms of α-carboxysomes and provides the framework for reprogramming carboxysome structures for synthetic biology and biotechnological applications. |
| title | Structure and encapsulation of carbonic anhydrase within the α-carboxysome. |
| topic | Carbonic Anhydrases Ribulose-Bisphosphate Carboxylase Carbon Dioxide Halothiobacillus Bacterial Proteins Protein Multimerization Carbon Cycle Cryoelectron Microscopy Microscopy, Electron, Transmission |
| url | https://pubmed.ncbi.nlm.nih.gov/41223214/ |