7N6H

The crystal structure of the GH30 subfamily 10 enzyme, AcXbh30A from Acetivibrio clariflavus

7N6H の概要

• エントリーDOI: 10.2210/pdb7n6h/pdb
• 分子名称: AcXbh30A, CHLORIDE ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: gh30, hydrolase
• 由来する生物種: Acetivibrio clariflavus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101149.40

構造登録者

Tan, K.,St John, F.J. (登録日: 2021-06-08, 公開日: 2022-08-17, 最終更新日: 2023-10-18)

主引用文献

St John, F.J.,Crooks, C.,Kim, Y.,Tan, K.,Joachimiak, A.
The first crystal structure of a xylobiose-bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase family 30, subfamily 10.
Febs Lett., 596:2449-2464, 2022

PubMed Abstract: Xylobiose is a prebiotic sugar that has applications in functional foods. This report describes the first X-ray crystallographic structure models of apo and xylobiose-bound forms of a xylobiohydrolase (XBH) from Acetivibrio clariflavus. This xylan-active enzyme, a member of the recently described glycoside hydrolase family 30 (GH30), subfamily 10, phylogenetic clade has been shown to strictly release xylobiose as its primary hydrolysis product. Inspection of the apo structure reveals a glycone region X -binding slot. When X binds, the non-reducing xylose in the -2 subsite is highly coordinated with numerous hydrogen bond contacts while contacts in the -1 subsite mostly reflect interactions typical for GH30 and enzymes in clan A of the carbohydrate-active enzymes database (CAZy). This structure provides an explanation for the high functional specificity of this new bacterial GH30 XBH subfamily.

PubMed: 35876256
DOI: 10.1002/1873-3468.14454

実験手法

X-RAY DIFFRACTION (1.28 Å)