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Open AccessJournal ArticleDOI

Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat.

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TLDR
This model of CotA contains all the structural features of a laccase, including the reactive surface-exposed copper center (T1) and two buried copper centers (T2 and T3), and shows a half-life of inactivation at 80 °C of about 4 and 2 h, indicating that CotA is intrinsically highly thermostable.
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This article is published in Journal of Biological Chemistry.The article was published on 2002-05-24 and is currently open access. It has received 502 citations till now. The article focuses on the topics: Endospore coat & Multicopper oxidase.

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Journal ArticleDOI

Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes

TL;DR: The addition of 5 mM CuSO4 was proven effective in triggering CueO activity at need with minor toxic effects on E. coli cells, and Cu‐treated E‐treated CueO cells were able to convert several phenolic compounds to the corresponding dimers.
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Evaluation of soil microbial communities and enzyme activities in cucumber continuous cropping soil treated with spent mushroom (Flammulina velutipes) substrate

TL;DR: In this article, the effects of spent Flammulina velutipes substrate (SFS) amendment on microbial properties of cucumber continuous cropping soil were assessed by denaturing gradient gel electrophoresis (DGGE) and real-time quantitative PCR.

In silico Analysis for Laccase-mediated Bioremediation of the Emerging Pharmaceutical Pollutants

TL;DR: The docking analysis approach can be useful in prediction of binding competence of pharmaceutical pollutants with l Accase for in situ laccase-mediated bioremediation.
Journal ArticleDOI

Diffraction pattern of Bacillus subtilis CotY spore coat protein 2D crystals.

TL;DR: Obtaining diffractions of 2D crystals pave the way to determination of 3D structure of coat proteins by using strong X-ray sources.
Journal ArticleDOI

Activity enhancement of CotA laccase by hydrophilic engineering, histidine tag optimization and static culture.

TL;DR: In this study, histidine tag position optimization and hydrophilic engineering were applied to increase the yield and activity of CotA protein.
References
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Journal ArticleDOI

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
Journal ArticleDOI

PROCHECK: a program to check the stereochemical quality of protein structures

TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
Journal ArticleDOI

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
Journal ArticleDOI

Comparative Protein Modelling by Satisfaction of Spatial Restraints

TL;DR: A comparative protein modelling method designed to find the most probable structure for a sequence given its alignment with related structures, which is automated and illustrated by the modelling of trypsin from two other serine proteinases.
Book ChapterDOI

Raster3D: photorealistic molecular graphics.

TL;DR: Raster3D is discussed, which is a suite of programs for molecular graphics, which must compromise the quality of rendered images to achieve rendering speeds high enough for useful interactive manipulation of three-dimensional objects.
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