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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

Chemical and thermal stabilization of CotA laccase via a novel one-step expression and immobilization in muNS-Mi nanospheres.

TL;DR: A methodology that programs eukaryotic or bacterial cells to encapsulate proteins of any kind inside micro/nanospheres formed by muNS-Mi viral protein was developed in this paper.
Journal ArticleDOI

Biochemical characterization of a thermostable cobalt- or copper-dependent polyphenol oxidase with dye decolorizing ability from Geobacillus sp. JS12.

TL;DR: This is the first report of a novel thermostable polyphenol oxidase that shows the cobalt-dependent laccase activity and dye decolorization ability.
Journal ArticleDOI

A novel laccase with urate oxidation activity from Lysobacter sp. T-15.

TL;DR: A unique urate-oxidizing enzyme was identified in a bacterium, strain T-15, and it was deemed to be a member of laccase from its broad substrate specificity, however, typical lacc enzyme and other multi-copper oxidases such as bilirubin oxidase and ascorbate oxidase seldom exhibit urate oxidation activity.
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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