Mapping the deformability of natural and designed cellulosomes in solution.
Bionanomachinery
Designer cellulosomes
Molecular modeling
Multi-enzyme complex
SAXS
Scaffoldins
Self-assembly
Journal
Biotechnology for biofuels and bioproducts
ISSN: 2731-3654
Titre abrégé: Biotechnol Biofuels Bioprod
Pays: England
ID NLM: 9918300888906676
Informations de publication
Date de publication:
20 Jun 2022
20 Jun 2022
Historique:
received:
06
12
2021
accepted:
08
06
2022
entrez:
20
6
2022
pubmed:
21
6
2022
medline:
21
6
2022
Statut:
epublish
Résumé
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. 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 R 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.
Sections du résumé
BACKGROUND
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
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 R
CONCLUSIONS
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.
Identifiants
pubmed: 35725490
doi: 10.1186/s13068-022-02165-3
pii: 10.1186/s13068-022-02165-3
pmc: PMC9210761
doi:
Types de publication
Journal Article
Langues
eng
Pagination
68Subventions
Organisme : Narodowym Centrum Nauki
ID : 2016/21/B/NZ1/00006
Organisme : FP7 Nanosciences, Nanotechnologies, Materials and new Production Technologies
ID : 604530
Organisme : FP7 Nanosciences, Nanotechnologies, Materials and new Production Technologies
ID : 604530
Organisme : FP7 Nanosciences, Nanotechnologies, Materials and new Production Technologies
ID : 604530
Organisme : ADEME ERANET IB
ID : 1201C0104
Informations de copyright
© 2022. The Author(s).
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