Cited by 190Photosynthetic Processes and MechanismsEnzyme Structure and FunctionMetalloenzymes and iron-sulfur proteins

Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

Mueller-Cajar, Oliver, Stotz, Mathias, Wendler, Petra, Hartl, F. Ulrich, Bracher, Andreas, Hayer-Hartl, Manajit·2011·Nature

Abstract

Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the fixation of atmospheric CO(2) in photosynthesis, but tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP). In plants, Rubisco is reactivated by the AAA(+) (ATPases associated with various cellular activities) protein Rubisco activase (Rca), but no such protein is known for the Rubisco of red algae. Here we identify the protein CbbX as an activase of red-type Rubisco. The 3.0-Å crystal structure of unassembled CbbX from Rhodobacter sphaeroides revealed an AAA(+) protein architecture. Electron microscopy and biochemical analysis showed that ATP and RuBP must bind to convert CbbX into functionally active, hexameric rings. The CbbX ATPase is strongly stimulated by RuBP and Rubisco. Mutational analysis suggests that CbbX functions by transiently pulling the carboxy-terminal peptide of the Rubisco large subunit into the hexamer pore, resulting in the release of the inhibitory RuBP. Understanding Rubisco activation may facilitate efforts to improve CO(2) uptake and biomass production by photosynthetic organisms.

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Crossref · 10.1038/nature10568

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Authors
Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M.
Affiliations
  • Max Planck Institute of Biochemistry (DE)
  • Ludwig-Maximilians-Universität München (DE)
Corresponding author
  • Bracher, Andreas
  • Hayer-Hartl, Manajit
Venue
Nature
Published
2011-11
Volume
479
Issue
7372
Pages
194-199
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
OpenAlex
W1982129514
Cited by
190
References
60
Citations by year
2026: 7 · 2025: 10 · 2024: 7 · 2023: 7 · 2022: 18 · 2021: 12 · 2020: 11 · 2019: 11 · 2018: 12 · 2017: 24 · 2016: 10 · 2015: 15 · 2014: 17 · 2013: 18 · 2012: 6
FWCI
5.84
Type
journal article
Language
en
Open access
closed
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
Funders
  • Deutsche Forschungsgemeinschaft
  • European Synchrotron Radiation Facility
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords
Rubisco activase, Rubisco, AAA+ ATPase, red algae, Rhodobacter sphaeroides, Rubisco activation, ribulose-1,5-bisphosphate, carboxy-terminal peptide, CO2 fixation, photosynthesis, protein crystal structure
MeSH terms
Adenosine Triphosphate, Allosteric Regulation, Bacterial Proteins, Carbon Dioxide, Enzyme Activation, Models, Molecular, Rhodobacter sphaeroides, Ribulose-Bisphosphate Carboxylase, Ribulosephosphates, Structure-Activity Relationship, Crystallography, X-Ray, Protein Structure, Quaternary, Protein Multimerization

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