5Z1X

Crystal Structure of Laccase from Cerrena sp. RSD1

5Z1X の概要

• エントリーDOI: 10.2210/pdb5z1x/pdb
• 分子名称: Laccase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: laccase, copper-dependent enzyme, oxidoreductase
• 由来する生物種: Cerrena sp. RSD1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108746.17

構造登録者

Lee, C.C.,Wu, M.H.,Ho, T.H.,Wang, A.H.J. (登録日: 2017-12-28, 公開日: 2018-09-05, 最終更新日: 2024-11-06)

主引用文献

Wu, M.H.,Lee, C.C.,Hsiao, A.S.,Yu, S.M.,Wang, A.H.J.,Ho, T.D.
Kinetic analysis and structural studies of a high-efficiency laccase fromCerrenasp. RSD1.
FEBS Open Bio, 8:1230-1246, 2018

PubMed Abstract: A high-efficiency laccase, DLac, was isolated from sp. RSD1. The kinetic studies indicate that DLac is a diffusion-limited enzyme. The crystal structure of DLac was determined to atomic resolution, and its overall structure shares high homology to monomeric laccases, but displays unique substrate-binding loops from those in other laccases. The substrate-binding residues with small side chain and the short substrate-binding loop IV broaden the substrate-binding cavity and may facilitate large substrate diffusion. Unlike highly glycosylated fungal laccases, the less-glycosylated DLac contains one highly conserved glycosylation site at N432 and an unique glycosylation site at N468. The -glycans stabilize the substrate-binding loops and the protein structure, and the first -acetylglucosamine is crucial for the catalytic efficiency. Additionally, a fivefold increase in protein yield is achieved via the submerged culture method for industrial applications.

PubMed: 30087829
DOI: 10.1002/2211-5463.12459

実験手法

X-RAY DIFFRACTION (1.38 Å)