ArticleThe Journal of biological chemistry2012
Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 37 citations in OpenAlex.
- Integrative SAXS and AFM analysis of engineered carbohydrate-active enzyme assemblies with tunable spatial organization.Protein science : a publication of the Protein Society · 2026Article
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- A cellulosomal double-dockerin module from Clostridium thermocellum shows distinct structural and cohesin-binding features.Protein science : a publication of the Protein Society · 2024Article
- Mechanochemical Coupling of Catalysis and Motion in a Cellulose-Degrading Multienzyme Nanomachine.ACS catalysis · 2024Article
- The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing.Proteins · 2022Article
- Mapping the deformability of natural and designed cellulosomes in solution.Biotechnology for biofuels and bioproducts · 2022Article
- Article
- Research progress and the biotechnological applications of multienzyme complex.Applied microbiology and biotechnology · 2021Review
- Cellulosomes: Highly Efficient Cellulolytic Complexes.Sub-cellular biochemistry · 2021Review
- Dynamic interactions of type I cohesin modules fine-tune the structure of the cellulosome ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction.Scientific reports · 2018Article
- Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Scientific reports · 2018Article
- Cellulosomes: bacterial nanomachines for dismantling plant polysaccharides.Nature reviews. Microbiology · 2017Review
- Article
- Stoichiometric Assembly of the Cellulosome Generates Maximum Synergy for the Degradation of Crystalline Cellulose, as Revealed by In Vitro Reconstitution of the Clostridium thermocellum Cellulosome.Applied and environmental microbiology · 2015Article
- Enhanced sampling techniques in molecular dynamics simulations of biological systems.Biochimica et biophysica acta · 2015Review
- Combining free and aggregated cellulolytic systems in the cellulosome-producing bacterium Ruminiclostridium cellulolyticum.Biotechnology for biofuels · 2015Article
- Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Atypical cohesin-dockerin complex responsible for cell surface attachment of cellulosomal components: binding fidelity, promiscuity, and structural buttresses.The Journal of biological chemistry · 2013Article
- Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Cellulosomes are multienzyme complexes responsible for efficient degradation of plant cell wall polysaccharides. The nonenzymatic scaffoldin subunit provides a platform for cellulolytic enzyme binding that enhances the overall activity of the bound enzymes. Understanding the unique quaternary structural elements responsible for the enzymatic synergy of the cellulosome is hindered by the large size and inherent flexibility of these multiprotein complexes. Herein, we have used x-ray crystallography and small angle x-ray scattering to structurally characterize a ternary protein complex from the Clostridium thermocellum cellulosome that comprises a C-terminal trimodular fragment of the CipA scaffoldin bound to the SdbA type II cohesin module and the type I dockerin module from the Cel9D glycoside hydrolase. This complex represents the largest fragment of the cellulosome solved by x-ray crystallography to date and reveals two rigid domains formed by the type I cohesin·dockerin complex and by the X module-type II cohesin·dockerin complex, which are separated by a 13-residue linker in an extended conformation. The type I dockerin modules of the four structural models found in the asymmetric unit are in an alternate orientation to that previously observed that provides further direct support for the dual mode of binding. Conserved intermolecular contacts between symmetry-related complexes were also observed and may play a role in higher order cellulosome structure. SAXS analysis of the ternary complex revealed that the 13-residue intermodular linker of the scaffoldin subunit is highly dynamic in solution. These studies provide fundamental insights into modular positioning, linker flexibility, and higher order organization of the cellulosome.
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