ArticleeLife2015
Resolving dual binding conformations of cellulosome cohesin-dockerin complexes using single-molecule force spectroscopy.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Engineering an artificial catch bond using mechanical anisotropy.Nature communications · 2024Article
- Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Influence of Fluorination on Single-Molecule Unfolding and Rupture Pathways of a Mechanostable Protein Adhesion Complex.Nano letters · 2020Article
- High force catch bond mechanism of bacterial adhesion in the human gut.Nature communications · 2020Article
- Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Mechanisms of Nanonewton Mechanostability in a Protein Complex Revealed by Molecular Dynamics Simulations and Single-Molecule Force Spectroscopy.Journal of the American Chemical Society · 2019Article
- Dual binding mode of "bitter sugars" to their human bitter taste receptor target.Scientific reports · 2019Article
- Engineered Stochastic Adhesion Between Microbes as a Protection Mechanism Against Environmental Stress.Cellular and molecular bioengineering · 2018Article
- Ligand Binding Stabilizes Cellulosomal Cohesins as Revealed by AFM-based Single-Molecule Force Spectroscopy.Scientific reports · 2018Article
- Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Scientific reports · 2018Article
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- Global Distribution Patterns and Pangenomic Diversity of the Candidate Phylum "Latescibacteria" (WS3).Applied and environmental microbiology · 2017Article
- Molecular origins of reduced activity and binding commitment of processive cellulases and associated carbohydrate-binding proteins to cellulose III.The Journal of biological chemistryArticle
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Authors and funding
8 authors.
Funding
Abstract
Receptor-ligand pairs are ordinarily thought to interact through a lock and key mechanism, where a unique molecular conformation is formed upon binding. Contrary to this paradigm, cellulosomal cohesin-dockerin (Coh-Doc) pairs are believed to interact through redundant dual binding modes consisting of two distinct conformations. Here, we combined site-directed mutagenesis and single-molecule force spectroscopy (SMFS) to study the unbinding of Coh:Doc complexes under force. We designed Doc mutations to knock out each binding mode, and compared their single-molecule unfolding patterns as they were dissociated from Coh using an atomic force microscope (AFM) cantilever. Although average bulk measurements were unable to resolve the differences in Doc binding modes due to the similarity of the interactions, with a single-molecule method we were able to discriminate the two modes based on distinct differences in their mechanical properties. We conclude that under native conditions wild-type Doc from Clostridium thermocellum exocellulase Cel48S populates both binding modes with similar probabilities. Given the vast number of Doc domains with predicted dual binding modes across multiple bacterial species, our approach opens up new possibilities for understanding assembly and catalytic properties of a broad range of multi-enzyme complexes.
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