ArticleScientific reports2015
Structural Characterization of a Newly Identified Component of α-Carboxysomes: The AAA+ Domain Protein CsoCbbQ.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 54 citations in OpenAlex.
- From fundamental understanding to engineering of carboxysomes for biotechnological applications.Plant communications · 2026Review
- Recent insights into α-carboxysome structure, mechanism, and assembly.Journal of bacteriology · 2026Review
- Structural modeling and biochemical characterization of MSMEG_0748, a MoxR ATPase fromComputational and structural biotechnology journal · 2025Article
- Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP.Science advances · 2024Article
- Identification of a carbonic anhydrase-Rubisco complex within the alpha-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.Frontiers in molecular biosciences · 2023Review
- Structome: a tool for the rapid assembly of datasets for structural phylogenetics.Bioinformatics advances · 2023Article
- Decoding the Absolute Stoichiometric Composition and Structural Plasticity of α-Carboxysomes.mBio · 2022Article
- The MIDAS domain of AAA mechanoenzyme Mdn1 forms catch bonds with two different substrates.eLife · 2022Article
- Incorporation of Functional Rubisco Activases into Engineered Carboxysomes to Enhance Carbon Fixation.ACS synthetic biology · 2022Article
- Dissolved Inorganic Carbon-Accumulating Complexes from Autotrophic Bacteria from Extreme Environments.Journal of bacteriology · 2021Article
- New discoveries expand possibilities for carboxysome engineering.Current opinion in microbiology · 2021Review
- Functional reconstitution of a bacterial COeLife · 2020Article
- Long-range intramolecular allostery and regulation in the dynein-like AAA protein Mdn1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.Communications biology · 2020Article
- Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Diversity in COApplied and environmental microbiology · 2019Article
- Assembly-disassembly is coupled to the ATPase cycle of tobacco Rubisco activase.The Journal of biological chemistry · 2018Article
- Carboxysome encapsulation of the CONature communications · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carboxysomes are bacterial microcompartments that enhance carbon fixation by concentrating ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and its substrate CO2 within a proteinaceous shell. They are found in all cyanobacteria, some purple photoautotrophs and many chemoautotrophic bacteria. Carboxysomes consist of a protein shell that encapsulates several hundred molecules of RuBisCO, and contain carbonic anhydrase and other accessory proteins. Genes coding for carboxysome shell components and the encapsulated proteins are typically found together in an operon. The α-carboxysome operon is embedded in a cluster of additional, conserved genes that are presumably related to its function. In many chemoautotrophs, products of the expanded carboxysome locus include CbbO and CbbQ, a member of the AAA+ domain superfamily. We bioinformatically identified subtypes of CbbQ proteins and show that their genes frequently co-occur with both Form IA and Form II RuBisCO. The α-carboxysome-associated ortholog, CsoCbbQ, from Halothiobacillus neapolitanus forms a hexamer in solution and hydrolyzes ATP. The crystal structure shows that CsoCbbQ is a hexamer of the typical AAA+ domain; the additional C-terminal domain, diagnostic of the CbbQ subfamily, structurally fills the inter-monomer gaps, resulting in a distinctly hexagonal shape. We show that CsoCbbQ interacts with CsoCbbO and is a component of the carboxysome shell, the first example of ATPase activity associated with a bacterial microcompartment.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.