5Z3K

Crystal structure of glucosidase from Croceicoccus marinus at 1.8 Angstrom resolution

5Z3K の概要

• エントリーDOI: 10.2210/pdb5z3k/pdb
• 分子名称: glucosidase, GLYCEROL (3 entities in total)
• 機能のキーワード: glycoside hydrolase, glucosidase, gh39, croceicoccus marinus, hydrolase
• 由来する生物種: Croceicoccus marinus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108280.60

構造登録者

Shen, Y.F.,Hu, X.J.,Li, J.X. (登録日: 2018-01-08, 公開日: 2019-01-23, 最終更新日: 2024-11-06)

主引用文献

Shen, Y.,Li, Z.,Huo, Y.Y.,Bao, L.,Gao, B.,Xiao, P.,Hu, X.,Xu, X.W.,Li, J.
Structural and Functional Insights Into CmGH1, a Novel GH39 Family beta-Glucosidase From Deep-Sea Bacterium.
Front Microbiol, 10:2922-2922, 2019

PubMed Abstract: Glucosidases play key roles in many diseases and are limiting enzymes during cellulose degradation, which is an important part of global carbon cycle. Here, we identified a novel β-glucosidase, CmGH1, isolated from marine bacterium E4A9. In spite of its high sequence and structural similarity with β-xylosidase family members, CmGH1 had enzymatic activity toward -nitrophenyl-β-D-glucopyranoside (NPG) and cellobiose. The and values of CmGH1 toward NPG were 0.332 ± 0.038 mM and 2.15 ± 0.081 min, respectively. CmGH1 was tolerant to high concentration salts, detergents, as well as many kinds of organic solvents. The crystal structure of CmGH1 was resolved with a 1.8 Å resolution, which showed that CmGH1 was composed of a canonical (α/β)-barrel catalytic domain and an auxiliary β-sandwich domain. Although no canonical catalytic triad residues were found in CmGH1, structural comparison and mutagenesis analysis suggested that residues Gln157 and Tyr264 of CmGH1 were the active sites. Mutant Q157E significantly increased its hydrolase activity up to 15-fold, whereas Y264E totally abolished its enzymatic activity. These results might provide new insights into understanding the different catalytic mechanism during evolution for β-glucosidases and β-xylosidases.

PubMed: 31921083
DOI: 10.3389/fmicb.2019.02922

実験手法

X-RAY DIFFRACTION (1.802 Å)