5NQ8

Crystal structure of laccases from Pycnoporus sanguineus, izoform II

5NQ8 の概要

• エントリーDOI: 10.2210/pdb5nq8/pdb
• 分子名称: Laccase, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: oxidoreductase, thermostable lacasses
• 由来する生物種: Pycnoporus coccineus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58200.10

構造登録者

Orlikowska, M.,de J.Rostro-Alanis, M.,Bujacz, A.,Hernandez-Luna, C.,Rubio, R.,Parra, R.,Bujacz, G. (登録日: 2017-04-19, 公開日: 2017-11-01, 最終更新日: 2024-11-06)

主引用文献

Orlikowska, M.,de J Rostro-Alanis, M.,Bujacz, A.,Hernandez-Luna, C.,Rubio, R.,Parra, R.,Bujacz, G.
Structural studies of two thermostable laccases from the white-rot fungus Pycnoporus sanguineus.
Int. J. Biol. Macromol., 107:1629-1640, 2018

PubMed Abstract: Laccases are enzymes that have the ability to catalyze the oxidation of a wide spectrum of phenolic compounds with the four-electron reduction of molecular oxygen to water. The active site of those proteins contains four copper ions, classified into three types. Laccases are interesting enzymes for study from the point of view of their structure, function and application because of their role in lignin degradation. Structural studies of two thermostable laccases produced by the strain Pycnoporus sanguineus CS43 (PsLacI and PsLacII) were performed. Both isoforms of PsLac show high thermal stability, at 60°C and 50°C, respectively, and they remained active at a high concentration of organic solvents. However, PsLacI has a higher thermal and pH stability and tolerance against inhibitors, and is a more efficient catalyst for ABTS and DMP (laccases substrate) than PsLacII. Based on the determined crystal structures we achieved insights into the structural factors relevant for the enzymatic properties of PsLacI and PsLacII. N-glycosylation site Asn354, which is very often present in structures of fungal laccases from other species, was not present in PsLac. This observation may be of particular significance due to the close distance between Asn354 and the substrate-binding pocket. This results in better access to the hydrophobic cavity for a particular substrate. Furthermore, we identified significant differences in the region of substrate-binding pocket, which confer PsLacI a markedly better performance than PsLacII.

PubMed: 29055703
DOI: 10.1016/j.ijbiomac.2017.10.024

実験手法

X-RAY DIFFRACTION (2 Å)