ArticleThe Journal of biological chemistry2015
Crucial roles of single residues in binding affinity, specificity, and promiscuity in the cellulosomal cohesin-dockerin interface.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Lignocellulose degradation in bacteria and fungi: cellulosomes and industrial relevance.Frontiers in microbiology · 2025Review
- Diverging co-translational protein complex assembly pathways are governed by interface energy distribution.Nature communications · 2024Article
- Article
- Impact of Structural Observables From Simulations to Predict the Effect of Single-Point Mutations in MHC Class II Peptide Binders.Frontiers in molecular biosciences · 2021Article
- Cellulosomes: Highly Efficient Cellulolytic Complexes.Sub-cellular biochemistry · 2021Review
- Article
- Isopod holobionts as promising models for lignocellulose degradation.Biotechnology for biofuels · 2020Article
- Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Scientific reports · 2018Article
- FlexPepDock lessons from CAPRI peptide-protein rounds and suggested new criteria for assessment of model quality and utility.Proteins · 2017Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interactions between cohesin and dockerin modules play a crucial role in the assembly of multienzyme cellulosome complexes. Although intraspecies cohesin and dockerin modules bind in general with high affinity but indiscriminately, cross-species binding is rare. Here, we combined ELISA-based experiments with Rosetta-based computational design to evaluate the contribution of distinct residues at the Clostridium thermocellum cohesin-dockerin interface to binding affinity, specificity, and promiscuity. We found that single mutations can show distinct and significant effects on binding affinity and specificity. In particular, mutations at cohesin position Asn(37) show dramatic variability in their effect on dockerin binding affinity and specificity: the N37A mutant binds promiscuously both to cognate (C. thermocellum) as well as to non-cognate Clostridium cellulolyticum dockerin. N37L in turn switches binding specificity: compared with the wild-type C. thermocellum cohesin, this mutant shows significantly increased preference for C. cellulolyticum dockerin combined with strongly reduced binding to its cognate C. thermocellum dockerin. The observation that a single mutation can overcome the naturally observed specificity barrier provides insights into the evolutionary dynamics of this system that allows rapid modulation of binding specificity within a high affinity background.
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