5D8Z

Structrue of a lucidum protein

5D8Z の概要

• エントリーDOI: 10.2210/pdb5d8z/pdb
• 関連するPDBエントリー: 5D8W
• 関連するBIRD辞書のPRD_ID: PRD_900005
• 分子名称: endoglucanase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: gh5 family, ganoderma lucidum, endoglucanase, hydrolase
• 由来する生物種: Ganoderma lucidum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74160.59

構造登録者

Guo, R.,Li, Q.,Shang, N.,Liu, G.,Ko, T.P.,Chen, C.C.,Liu, W. (登録日: 2015-08-18, 公開日: 2016-06-29, 最終更新日: 2024-10-09)

主引用文献

Liu, G.,Li, Q.,Shang, N.,Huang, J.W.,Ko, T.P.,Liu, W.,Zheng, Y.,Han, X.,Chen, Y.,Chen, C.C.,Jin, J.,Guo, R.T.
Functional and structural analyses of a 1,4-beta-endoglucanase from Ganoderma lucidum.
Enzyme.Microb.Technol., 86:67-74, 2016

PubMed Abstract: Ganoderma lucidum is a saprotrophic white-rot fungus which contains a rich set of cellulolytic enzymes. Here, we screened an array of potential 1,4-β-endoglucanases from G. lucidum based on the gene annotation library and found that one candidate gene, GlCel5A, exhibits CMC-hydrolyzing activity. The recombinant GlCel5A protein expressed in Pichia pastoris is able to hydrolyze CMC and β-glucan but not xylan and mannan. The enzyme exhibits optimal activity at 60°C and pH 3-4, and retained 50% activity at 80 and 90°C for at least 15 and 10min. The crystal structure of GlCel5A and its complex with cellobiose, solved at 2.7 and 2.86Å resolution, shows a classical (β/α)8 TIM-barrel fold as seen in other members of glycoside hydrolase family 5. The complex structure contains a cellobiose molecule in the +1 and +2 subsites, and reveals the interactions with the positive sites of the enzyme. Collectively, the present work provides the first comprehensive characterization of an endoglucanase from G. lucidum that possesses properties for industrial applications, and strongly encourages further studying in the cellulolytic enzyme system of G. lucidum.

PubMed: 26992795
DOI: 10.1016/j.enzmictec.2016.01.013

実験手法

X-RAY DIFFRACTION (2.7 Å)