Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site

Liu, Zhongchuan; Xie, Tian; Zhong, Qiuping; Wang, Ganggang

doi:10.1107/s2053230x1600426x

Cited by 27 publications

(16 citation statements)

References 41 publications

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“…Ba L displays a fourth disulphide bridge between Cys201-Cys209 that seems to stabilize an extended loop (see Fig 5 ). Among Mt L, Ma L and Ta L, the largest structural variations are observed for domain C. Most pronounced in the loop regions near the T1-substrate binding pocket (365–369, 424–429, 452–457) and the loops (410–414, 460–469, 347–351) near the putative, novel binding site described for ABTS [ 9 ] (see Fig 3 ).…”

Section: Resultsmentioning

confidence: 99%

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A comparative structural analysis of the surface properties of asco-laccases

et al. 2018

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Laccases of different biological origins have been widely investigated and these studies have elucidated fundamentals of the generic catalytic mechanism. However, other features such as surface properties and residues located away from the catalytic centres may also have impact on enzyme function. Here we present the crystal structure of laccase from Myceliophthora thermophila (MtL) to a resolution of 1.62 Å together with a thorough structural comparison with other members of the CAZy family AA1_3 that comprises fungal laccases from ascomycetes. The recombinant protein produced in A. oryzae has a molecular mass of 75 kDa, a pI of 4.2 and carries 13.5 kDa N-linked glycans. In the crystal, MtL forms a dimer with the phenolic substrate binding pocket blocked, suggesting that the active form of the enzyme is monomeric. Overall, the MtL structure conforms with the canonical fold of fungal laccases as well as the features specific for the asco-laccases. However, the structural comparisons also reveal significant variations within this taxonomic subgroup. Notable differences in the T1-Cu active site topology and polar motifs imply molecular evolution to serve different functional roles. Very few surface residues are conserved and it is noticeable that they encompass residues that interact with the N-glycans and/or are located at domain interfaces. The N-glycosylation sites are surprisingly conserved among asco-laccases and in most cases the glycan displays extensive interactions with the protein. In particular, the glycans at Asn88 and Asn210 appear to have evolved as an integral part of the asco-laccase structure. An uneven distribution of the carbohydrates around the enzyme give unique properties to a distinct part of the surface of the asco-laccases which may have implication for laccase function–in particular towards large substrates.

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Section: Resultsmentioning

confidence: 99%

“…The size and topology of the T1 pocket vary significantly between phylogenetic subclasses of laccases. The recent observation of a binding site for the non-phenolic substrate ABTS localized 26 Å from the T1 pocket in a bacterial laccase [ 9 ], adds to the complexity of laccase function.…”

Section: Introductionmentioning

confidence: 99%

A comparative structural analysis of the surface properties of asco-laccases

et al. 2018

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“…When avone (3) possesses two adjacent phenolic groups, the oxidation of these substrates could be catalyzed by laccase. Flavonols (5,6,7), isoavones (10,11) and chalcone (12) with one or more phenolic groups were the effective substrates of laccase. On the other hand, avanones (8, 9) could not be oxidated by laccase.…”

Section: Oxidation Of Avone Analogues Mediated By Oxidasesmentioning

confidence: 99%

“…EC 1.10.3.2), known as multi-copper oxidase, is widely distributed in natural sources, such as fungi, bacteria, plant, insects and lichens, with the molecular mass range of 50-130 kDa. 9,10 Laccases have a functional unit that consists of four coppers, which could catalyze the oxidation of various organic compounds, such as diphenols, polyphenols, diamines, aromatic amines, benzeneethiols, and substituted phenols ( Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic oxidation of flavone analogues mediated by general biocatalysts: horseradish peroxidase and laccase

et al. 2019

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“…Laccases are considered “moonlighting” proteins, owing to their multiple biological activities [108]. PDB structures of > 70 fungal and a few bacterial laccases have been reported, crystallized in their wild-type, mutant, and derivative forms, as well as complexed to a variety of substrate-like ligands and oxygen reactive species [109, 148]. This set of structures has shed light on their stabilities and functional characteristics, as described above.…”

Section: Structure Of Laccases and Comparative Structure Analysesmentioning

confidence: 99%

Laccases: structure, function, and potential application in water bioremediation

et al. 2019

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The global rise in urbanization and industrial activity has led to the production and incorporation of foreign contaminant molecules into ecosystems, distorting them and impacting human and animal health. Physical, chemical, and biological strategies have been adopted to eliminate these contaminants from water bodies under anthropogenic stress. Biotechnological processes involving microorganisms and enzymes have been used for this purpose; specifically, laccases, which are broad spectrum biocatalysts, have been used to degrade several compounds, such as those that can be found in the effluents from industries and hospitals. Laccases have shown high potential in the biotransformation of diverse pollutants using crude enzyme extracts or free enzymes. However, their application in bioremediation and water treatment at a large scale is limited by the complex composition and high salt concentration and pH values of contaminated media that affect protein stability, recovery and recycling. These issues are also associated with operational problems and the necessity of large-scale production of laccase. Hence, more knowledge on the molecular characteristics of water bodies is required to identify and develop new laccases that can be used under complex conditions and to develop novel strategies and processes to achieve their efficient application in treating contaminated water. Recently, stability, efficiency, separation and reuse issues have been overcome by the immobilization of enzymes and development of novel biocatalytic materials. This review provides recent information on laccases from different sources, their structures and biochemical properties, mechanisms of action, and application in the bioremediation and biotransformation of contaminant molecules in water. Moreover, we discuss a series of improvements that have been attempted for better organic solvent tolerance, thermo-tolerance, and operational stability of laccases, as per process requirements.

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Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site

Cited by 27 publications

References 41 publications

A comparative structural analysis of the surface properties of asco-laccases

A comparative structural analysis of the surface properties of asco-laccases

Biocatalytic oxidation of flavone analogues mediated by general biocatalysts: horseradish peroxidase and laccase

Laccases: structure, function, and potential application in water bioremediation

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