In this section
@article{Ng:2025:10.1073/pnas.2523723122,
author = {Ng, PC and Adegbite, O and Li, T and Baslé, A and Marles-Wright, J and Liu, L-N},
doi = {10.1073/pnas.2523723122},
journal = {Proc Natl Acad Sci U S A},
title = {Structure and encapsulation of carbonic anhydrase within the α-carboxysome.},
url = {http://dx.doi.org/10.1073/pnas.2523723122},
volume = {122},
year = {2025}
}
TY - JOUR
AB - Carboxysomes in cyanobacteria and certain proteobacteria enable efficient CO2 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 CO2 and HCO3-, supplying elevated levels of CO2 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 Halothiobacillus neapolitanus (HnCsoSCA). HnCsoSCA adopts a trimer-of-dimers oligomeric structure without the incorporation of a zinc ion at its symmetric center. Using synthetic minishells, we demonstrate that HnCsoSCA interacts with the CsoS1A shell hexamer and is incorporated into the minishells at the inner surface, independent of the CsoS2 linker protein. HnCsoSCA truncations suggest nonspecific interactions between HnCsoSCA and CsoS1A. We further show that HnCsoSCA 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.
AU - Ng,PC
AU - Adegbite,O
AU - Li,T
AU - Baslé,A
AU - Marles-Wright,J
AU - Liu,L-N
DO - 10.1073/pnas.2523723122
PY - 2025///
TI - Structure and encapsulation of carbonic anhydrase within the α-carboxysome.
T2 - Proc Natl Acad Sci U S A
UR - http://dx.doi.org/10.1073/pnas.2523723122
UR - https://www.ncbi.nlm.nih.gov/pubmed/41223214
VL - 122
ER -
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