Abstract

Background

Natural 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.

Results

We 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 Rg and Dmax values deduced from the scattering curves and corresponding molecular models highlight their variable aspects, depending on composition, size and spatial organization of the objects in solution.

Conclusions

Our 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.

Details

Title
Mapping the deformability of natural and designed cellulosomes in solution
Author
Dorival, Jonathan; Moraïs, Sarah; Labourel, Aurore; Rozycki, Bartosz; Pierre-Andre Cazade; Dabin, Jérôme; Setter-Lamed, Eva; Mizrahi, Itzhak; Thompson, Damien; Thureau, Aurélien; Bayer, Edward A; Czjzek, Mirjam  VIAFID ORCID Logo 
Pages
1-17
Section
Research
Publication year
2022
Publication date
2022
Publisher
BioMed Central
e-ISSN
1754-6834
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2691527836
Copyright
© 2022. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.