ArticleThe Journal of biological chemistry2010
Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Thermostable Bacterial Collagenolytic Proteases: A Review.Journal of microbiology and biotechnology · 2024Review
- The Phylogeny and Metabolic Potentials of a Lignocellulosic Material-DegradingMicroorganisms · 2024Article
- All DACs in a Row: Domain Architectures of Bacterial and Archaeal Diadenylate Cyclases.Journal of bacteriology · 2023Review
- Mechanistic Insight into the Fragmentation of Type I Collagen Fibers into Peptides and Amino Acids by aApplied and environmental microbiology · 2022Article
- Maturation Process and Characterization of a Novel Thermostable and Halotolerant Subtilisin-Like Protease with High Collagenolytic Activity but Low Gelatinolytic Activity.Applied and environmental microbiology · 2022Article
- Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.Nature communications · 2022Article
- Biochemical characterisation of a collagenase from Bacillus cereus strain Q1.Scientific reports · 2021Article
- Induction of posterior vitreous detachment (PVD) by non-enzymatic reagents targeting vitreous collagen liquefaction as well as vitreoretinal adhesion.Scientific reports · 2020Article
- Characterization of a New M4 Metalloprotease With Collagen-Swelling Ability From MarineFrontiers in microbiology · 2020Article
- Mechanistic Insight into the Binding and Swelling Functions of Prepeptidase C-Terminal (PPC) Domains from Various Bacterial Proteases.Applied and environmental microbiology · 2019Article
- Discovery of a Potent Inhibitor Class with High Selectivity toward Clostridial Collagenases.Journal of the American Chemical Society · 2017Article
- Article
- Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases.Applied and environmental microbiology · 2015Review
- Mechanistic insights into elastin degradation by pseudolysin, the major virulence factor of the opportunistic pathogen Pseudomonas aeruginosa.Scientific reports · 2015Article
- Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Development of an efficient conjugation-based genetic manipulation system for Pseudoalteromonas.Microbial cell factories · 2015Article
- Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen.Journal of proteomics · 2014Article
- Characterization of a novel subtilisin-like protease myroicolsin from deep sea bacterium Myroides profundi D25 and molecular insight into its collagenolytic mechanism.The Journal of biological chemistry · 2014Article
- The β-glucanase ZgLamA from Zobellia galactanivorans evolved a bent active site adapted for efficient degradation of algal laminarin.The Journal of biological chemistry · 2014Article
- Interstitial collagen catabolism.The Journal of biological chemistry · 2013Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Deseasin MCP-01 is a bacterial collagenolytic serine protease. Its catalytic domain alone can degrade collagen, and its C-terminal PKD domain is a collagen-binding domain (CBD) that can improve the collagenolytic efficiency of the catalytic domain by an unknown mechanism. Here, scanning electron microscopy (SEM), atomic force microscopy (AFM), zeta potential, and circular dichroism spectroscopy were used to clarify the functional mechanism of the PKD domain in MCP-01 collagenolysis. The PKD domain observably swelled insoluble collagen. Its collagen-swelling ability and its improvement to the collagenolysis of the catalytic domain are both temperature-dependent. SEM observation showed the PKD domain swelled collagen fascicles with an increase of their diameter from 5.3 mum to 8.8 mum after 1 h of treatment, and the fibrils forming the fascicles were dispersed. AFM observation directly showed that the PKD domain bound collagen, swelled the microfibrils, and exposed the monomers. The PKD mutant W36A neither bound collagen nor disturbed its structure. Zeta potential results demonstrated that PKD treatment increased the net positive charges of the collagen surface. PKD treatment caused no change in the content or the thermostability of the collagen triple helix. Furthermore, the PKD-treated collagen could not be degraded by gelatinase. Therefore, though the triple helix monomers were exposed, the PKD domain could not unwind the collagen triple helix. Our study reveals the functional mechanism of the PKD domain of the collagenolytic serine protease MCP-01 in collagen degradation, which is distinct from that of the CBDs of mammalian matrix metalloproteases.
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