ArticleProceedings of the National Academy of Sciences of the United States of America2009
On the remarkable mechanostability of scaffoldins and the mechanical clamp motif.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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48 citing papers in PubMed, 120 citations in OpenAlex.
- A minimal cellulosome-like system in Cellulosilyticum lentocellum.FEBS open bio · 2026Article
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- MechanoProDB: a web-based database for exploring the mechanical properties of proteins.Database : the journal of biological databases and curation · 2024Article
- Improvement of Cellulomonas fimi endoglucanase CenA by multienzymatic display on a decameric structural scaffold.Applied microbiology and biotechnology · 2023Article
- SPACA6 ectodomain structure reveals a conserved superfamily of gamete fusion-associated proteins.Communications biology · 2022Article
- Using steered molecular dynamic tension for assessing quality of computational protein structure models.Journal of computational chemistry · 2022Article
- Mapping Mechanostable Pulling Geometries of a Therapeutic Anticalin/CTLA-4 Protein Complex.Nano letters · 2022Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Divergent CPEB prion-like domains reveal different assembly mechanisms for a generic amyloid-like fold.BMC biology · 2021Article
- Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2020Article
- Essential role of calcium in extending RTX adhesins to their target.Journal of structural biology: X · 2020Article
- Substrate-Related Factors Affecting Cellulosome-Induced Hydrolysis for Lignocellulose Valorization.International journal of molecular sciences · 2019Review
- Enzymatic biosynthesis and immobilization of polyprotein verified at the single-molecule level.Nature communications · 2019Article
- Calcium stabilizes the strongest protein fold.Nature communications · 2018Article
- Mechanical architecture and folding of E. coli type 1 pilus domains.Nature communications · 2018Article
- Ligand Binding Stabilizes Cellulosomal Cohesins as Revealed by AFM-based Single-Molecule Force Spectroscopy.Scientific reports · 2018Article
- The cohesin module is a major determinant of cellulosome mechanical stability.The Journal of biological chemistry · 2018Article
- Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Scientific reports · 2018Article
- Combining in Vitro and in Silico Single-Molecule Force Spectroscopy to Characterize and Tune Cellulosomal Scaffoldin Mechanics.Journal of the American Chemical Society · 2017Article
- Cellulosomes: bacterial nanomachines for dismantling plant polysaccharides.Nature reviews. Microbiology · 2017Review
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein mechanostability is a fundamental biological property that can only be measured by single-molecule manipulation techniques. Such studies have unveiled a variety of highly mechanostable modules (mainly of the Ig-like, beta-sandwich type) in modular proteins subjected to mechanical stress from the cytoskeleton and the metazoan cell-cell interface. Their mechanostability is often attributed to a "mechanical clamp" of secondary structure (a patch of backbone hydrogen bonds) fastening their ends. Here we investigate the nanomechanics of scaffoldins, an important family of scaffolding proteins that assembles a variety of cellulases into the so-called cellulosome, a microbial extracellular nanomachine for cellulose adhesion and degradation. These proteins anchor the microbial cell to cellulose substrates, which makes their connecting region likely to be subjected to mechanical stress. By using single-molecule force spectroscopy based on atomic force microscopy, polyprotein engineering, and computer simulations, here we show that the cohesin I modules from the connecting region of cellulosome scaffoldins are the most robust mechanical proteins studied experimentally or predicted from the entire Protein Data Bank. The mechanostability of the cohesin modules studied correlates well with their mechanical kinetic stability but not with their thermal stability, and it is well predicted by computer simulations, even coarse-grained. This extraordinary mechanical stability is attributed to 2 mechanical clamps in tandem. Our findings provide the current upper limit of protein mechanostability and establish shear mechanical clamps as a general structural/functional motif widespread in proteins putatively subjected to mechanical stress. These data have important implications for the scaffoldin physiology and for protein design in biotechnology and nanotechnology.
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