ArticleNature communications2022
Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.
Article in Nature communications, 2022. 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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10 citing papers in PubMed, 29 citations in OpenAlex.
- Bacterial collagenase harnesses collagen geometry for processive cleavage.Nature communications · 2026Article
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- High Proteolytic and Collagenolytic Activity in an EnvironmentalInternational journal of molecular sciences · 2025Article
- Catechol redox maintenance in mussel adhesion.Nature reviews. Chemistry · 2025Review
- Antimicrobial Nanoparticles Composed of Zein and Arginine-Phenylalanine-Based Surfactants for Wound Related Infections: Antioxidant and Skin-Related Anti-Enzymatic Activities and Toxicity.Antibiotics (Basel, Switzerland) · 2024Article
- Thermostable Bacterial Collagenolytic Proteases: A Review.Journal of microbiology and biotechnology · 2024Review
- Heparan sulfate selectively inhibits the collagenase activity of cathepsin K.Matrix biology : journal of the International Society for Matrix Biology · 2024Article
- A conserved strategy to attack collagen: The activator domain in bacterial collagenases unwinds triple-helical collagen.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Heparan sulfate selectively inhibits the collagenase activity of cathepsin K.bioRxiv : the preprint server for biology · 2024Article
- Unlocking the Potential of Collagenases: Structures, Functions, and Emerging Therapeutic Horizons.Biodesign research · 2024Article
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Authors and funding
15 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The collagenases of Vibrio species, many of which are pathogens, have been regarded as an important virulence factor. However, there is little information on the structure and collagenolytic mechanism of Vibrio collagenase. Here, we report the crystal structure of the collagenase module (CM) of Vibrio collagenase VhaC and the conformation of VhaC in solution. Structural and biochemical analyses and molecular dynamics studies reveal that triple-helical collagen is initially recognized by the activator domain, followed by subsequent cleavage by the peptidase domain along with the closing movement of CM. This is different from the peptidolytic mode or the proposed collagenolysis of Clostridium collagenase. We propose a model for the integrated collagenolytic mechanism of VhaC, integrating the functions of VhaC accessory domains and its collagen degradation pattern. This study provides insight into the mechanism of bacterial collagenolysis and helps in structure-based drug design targeting of the Vibrio collagenase.
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