ArticleBiophysical journal2013
Solution structure of clostridial collagenase H and its calcium-dependent global conformation change.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Bacterial collagenase harnesses collagen geometry for processive cleavage.Nature communications · 2026Article
- 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
- A novel computationally engineered collagenase reduces the force required for tooth extraction in an ex-situ porcine jaw model.Journal of biological engineering · 2023Article
- Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.Nature communications · 2022Article
- Evaluation of alternative diluents for clinical use of collagenase clostridium histolyticum (CCH-aaes).Journal of cosmetic dermatology · 2021Article
- Combinatorial approach for screening and assessment of multiple therapeutic enzymes from marine isolateRSC advances · 2019Article
- Article
- CaThe FEBS journal · 2018Article
- Collagen V Is a Potential Substrate for Clostridial Collagenase G in Pancreatic Islet Isolation.Journal of diabetes research · 2016Article
- Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen.Journal of proteomics · 2014Article
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Authors and funding
10 authors.
Funding
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Abstract
Collagenase H (ColH) from Clostridium histolyticum is a multimodular protein composed of a collagenase module (activator and peptidase domains), two polycystic kidney disease-like domains, and a collagen-binding domain. The interdomain conformation and its changes are very important for understanding the functions of ColH. In this study, small angle x-ray scattering and limited proteolysis were employed to reveal the interdomain arrangement of ColH in solution. The ab initio beads model indicated that ColH adopted a tapered shape with a swollen head. Under calcium-chelated conditions (with EGTA), the overall structure was further elongated. The rigid body model indicated that the closed form of the collagenase module was preferred in solution. The limited proteolysis demonstrated that the protease sensitivity of ColH was significantly increased under the calcium-chelated conditions, and that the digestion mainly occurred in the domain linker regions. Fluorescence measurements with a fluorescent dye were performed with the limited proteolysis products after separation. The results indicated that the limited proteolysis products exhibited fluorescence similar to that of the full-length ColH. These findings suggested that the conformation of full-length ColH in solution is the elongated form, and this form is calcium-dependently maintained at the domain linker regions.
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