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Identification of a...
Identification of a carbonic anhydrase-Rubisco complex within the alpha-carboxysome
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- Blikstad, Cecilia (author)
- Uppsala universitet,Molekylär biomimetik,Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA.,Mikrobiell Kemi
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- Dugan, Eli J. (author)
- Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA.
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- Laughlin, Thomas G. (author)
- Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA.
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- Turnsek, Julia B. (author)
- Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA.
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- Liu, Mira D. (author)
- Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA.
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- Shoemaker, Sophie R. (author)
- Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA.
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- Vogiatzi, Nikoleta (author)
- Uppsala universitet,Molekylär biomimetik,Mikrobiell Kemi
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- Remis, Jonathan P. (author)
- Univ Calif Berkeley, Calif Inst Quantitat Biosci, Berkeley, CA 94720 USA.
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- Savage, David F. (author)
- Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA.;Univ Calif Berkeley, HHMI, Berkeley, CA 94720 USA.
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(creator_code:org_t)
- Proceedings of the National Academy of Sciences (PNAS), 2023
- 2023
- English.
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In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences (PNAS). - 0027-8424 .- 1091-6490. ; 120:43
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Abstract
Subject headings
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- Carboxysomes are proteinaceous organelles that encapsulate key enzymes of CO2 fixation-Rubisco and carbonic anhydrase-and are the centerpiece of the bacterial CO2 concentrating mechanism (CCM). In the CCM, actively accumulated cytosolic bicarbonate diffuses into the carboxysome and is converted to CO2 by carbonic anhydrase, producing a high CO2 concentration near Rubisco and ensuring efficient carboxylation. Self- assembly of the alpha-carboxysome is orchestrated by the intrinsically disordered scaffolding protein, CsoS2, which interacts with both Rubisco and carboxysomal shell proteins, but it is unknown how the carbonic anhydrase, CsoSCA, is incorporated into the alpha-carboxysome. Here, we present the structural basis of carbonic anhydrase encapsulation into alpha-carboxysomes from Halothiobacillus neapolitanus. We find that CsoSCA interacts directly with Rubisco via an intrinsically disordered N- terminal domain. A 1.98 angstrom single- particle cryoelectron microscopy structure of Rubisco in complex with this peptide reveals that CsoSCA binding is predominantly mediated by a network of hydrogen bonds. CsoSCA's binding site overlaps with that of CsoS2, but the two proteins utilize substantially different motifs and modes of binding, revealing a plasticity of the Rubisco binding site. Our results advance the understanding of carboxysome biogenesis and highlight the importance of Rubisco, not only as an enzyme but also as a central hub for mediating assembly through protein interactions.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- CO2 fixation
- carboxysome
- carbonic anhydrase
- protein-protein interactions
- cryoelectron microscopy
Publication and Content Type
- ref (subject category)
- art (subject category)
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