ArticleThe Journal of biological chemistry2011
Modeling the self-assembly of the cellulosome enzyme complex.
Article in The Journal of biological chemistry, 2011. 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, 52 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
- Deconstruction byLife science alliance · 2026Article
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Mapping the deformability of natural and designed cellulosomes in solution.Biotechnology for biofuels and bioproducts · 2022Article
- Article
- Characterisation of the Effect of the Spatial Organisation of Hemicellulases on the Hydrolysis of Plant Biomass Polymer.International journal of molecular sciences · 2020Article
- A Biological Nanomachine at Work: Watching the Cellulosome Degrade Crystalline Cellulose.ACS central science · 2020Article
- Substrate-Related Factors Affecting Cellulosome-Induced Hydrolysis for Lignocellulose Valorization.International journal of molecular sciences · 2019Review
- Growth and expression of relevant metabolic genes of Clostridium thermocellum cultured on lignocellulosic residues.Journal of industrial microbiology & biotechnology · 2017Article
- Complexity of the Ruminococcus flavefaciens FD-1 cellulosome reflects an expansion of family-related protein-protein interactions.Scientific reports · 2017Article
- 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
- Significance of relative position of cellulases in designer cellulosomes for optimized cellulolysis.PloS one · 2015Article
- Ultrastable cellulosome-adhesion complex tightens under load.Nature communications · 2014Article
- The emergence of Clostridium thermocellum as a high utility candidate for consolidated bioprocessing applications.Frontiers in chemistry · 2014Review
- A synthetic biology approach for evaluating the functional contribution of designer cellulosome components to deconstruction of cellulosic substrates.Biotechnology for biofuels · 2013Article
- Secretory pathway of cellulase: a mini-review.Biotechnology for biofuels · 2013Article
- Improved production of L-threonine in Escherichia coli by use of a DNA scaffold system.Applied and environmental microbiology · 2013Article
- Microbiology: Break down the walls.Nature · 2013Article
- Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most bacteria use free enzymes to degrade plant cell walls in nature. However, some bacteria have adopted a different strategy wherein enzymes can either be free or tethered on a protein scaffold forming a complex called a cellulosome. The study of the structure and mechanism of these large macromolecular complexes is an active and ongoing research topic, with the goal of finding ways to improve biomass conversion using cellulosomes. Several mechanisms involved in cellulosome formation remain unknown, including how cellulosomal enzymes assemble on the scaffoldin and what governs the population of cellulosomes created during self-assembly. Here, we present a coarse-grained model to study the self-assembly of cellulosomes. The model captures most of the physical characteristics of three cellulosomal enzymes (Cel5B, CelS, and CbhA) and the scaffoldin (CipA) from Clostridium thermocellum. The protein structures are represented by beads connected by restraints to mimic the flexibility and shapes of these proteins. From a large simulation set, the assembly of cellulosomal enzyme complexes is shown to be dominated by their shape and modularity. The multimodular enzyme, CbhA, binds statistically more frequently to the scaffoldin than CelS or Cel5B. The enhanced binding is attributed to the flexible nature and multimodularity of this enzyme, providing a longer residence time around the scaffoldin. The characterization of the factors influencing the cellulosome assembly process may enable new strategies to create designers cellulosomes.
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