ArticleActa crystallographica. Section F, Structural biology communications2016
Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. 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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16 citing papers in PubMed, 39 citations in OpenAlex.
- Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.Microorganisms · 2025Review
- Targets for the diagnosis ofmSphere · 2025Article
- Enhancement in the Catalytic Properties of CotA Laccase fromMicroorganisms · 2025Article
- Cellulose binding and the timing of expression influence protein targeting to the double-layered cyst wall ofmSphere · 2024Article
- Polymerization potential of a bacterial CotA-laccase for β-naphthol: enzyme structure and comprehensive polymer characterization.Frontiers in microbiology · 2024Article
- Molecular Docking of Lac_CB10: Highlighting the Great Potential for Bioremediation of Recalcitrant Chemical Compounds by One Predicted Bacteroidetes CopA-Laccase.International journal of molecular sciences · 2023Article
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Conversion of lignin-derived 3-methoxycatechol to the natural product purpurogallin using bacterial P450 GcoAB and laccase CueO.Applied microbiology and biotechnology · 2022Article
- Fungal Laccases: The Forefront of Enzymes for Sustainability.Journal of fungi (Basel, Switzerland) · 2021Review
- Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.Microbial biotechnology · 2021Article
- Enzymatic Oxidation of Ca-Lignosulfonate and Kraft Lignin in Different Lignin-Laccase-Mediator-Systems and MDF Production.Frontiers in bioengineering and biotechnology · 2021Article
- Balancing Enzyme Encapsulation Efficiency and Stability in Complex Coacervate Core Micelles.Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Laccases: structure, function, and potential application in water bioremediation.Microbial cell factories · 2019Review
- Biocatalytic oxidation of flavone analogues mediated by general biocatalysts: horseradish peroxidase and laccase.RSC advances · 2019Article
- Bacterial laccases: promising biological green tools for industrial applications.Cellular and molecular life sciences : CMLS · 2018Review
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4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The CotA laccase from Bacillus subtilis is an abundant component of the spore outer coat and has been characterized as a typical laccase. The crystal structure of CotA complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS) in a hole motif has been solved. The novel binding site was about 26 Å away from the T1 binding pocket. Comparison with known structures of other laccases revealed that the hole is a specific feature of CotA. The key residues Arg476 and Ser360 were directly bound to ABTS. Site-directed mutagenesis studies revealed that the residues Arg146, Arg429 and Arg476, which are located at the bottom of the novel binding site, are essential for the oxidation of ABTS and syringaldazine. Specially, a Thr480Phe variant was identified to be almost 3.5 times more specific for ABTS than for syringaldazine compared with the wild type. These results suggest this novel binding site for ABTS could be a potential target for protein engineering of CotA laccases.
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