ArticleBiotechnology for biofuels and bioproducts2022
Mapping the deformability of natural and designed cellulosomes in solution.
Article in Biotechnology for biofuels and bioproducts, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Alkaliphilic microbial cellulases: sources, structural insights, and bioengineering approaches for industrial applications.Archives of microbiology · 2026Review
- Integrative SAXS and AFM analysis of engineered carbohydrate-active enzyme assemblies with tunable spatial organization.Protein science : a publication of the Protein Society · 2026Article
- Lignocellulose degradation in bacteria and fungi: cellulosomes and industrial relevance.Frontiers in microbiology · 2025Review
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Scrutinising the Conformational Ensemble of the Intrinsically Mixed-Folded Protein Galectin-3.Molecules (Basel, Switzerland) · 2024Article
- Current challenges in designer cellulosome engineering.Applied microbiology and biotechnology · 2023Review
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 5 countries.
Funding
Abstract
backgroundNatural cellulosome multi-enzyme complexes, their components, and engineered 'designer cellulosomes' (DCs) promise an efficient means of breaking down cellulosic substrates into valuable biofuel products. Their broad uptake in biotechnology relies on boosting proximity-based synergy among the resident enzymes, but the modular architecture challenges structure determination and rational design.
resultsWe used small angle X-ray scattering combined with molecular modeling to study the solution structure of cellulosomal components. These include three dockerin-bearing cellulases with distinct substrate specificities, original scaffoldins from the human gut bacterium Ruminococcus champanellensis (ScaA, ScaH and ScaK) and a trivalent cohesin-bearing designer scaffoldin (Scaf20L), followed by cellulosomal complexes comprising these components, and the nonavalent fully loaded Clostridium thermocellum CipA in complex with Cel8A from the same bacterium. The size analysis of R
conclusionsOur data quantifies variability of form and compactness of cellulosomal components in solution and confirms that this native plasticity may well be related to speciation with respect to the substrate that is targeted. By showing that scaffoldins or components display enhanced compactness compared to the free objects, we provide new routes to rationally enhance their stability and performance in their environment of action.
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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.