6JBS

Bifunctional xylosidase/glucosidase LXYL

6JBS の概要

• エントリーDOI: 10.2210/pdb6jbs/pdb
• 分子名称: Beta-D-xylosidase/beta-D-glucosidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (12 entities in total)
• 機能のキーワード: glycoside hydrolases, xylosidases, bifunctional, hydrolase
• 由来する生物種: Lentinula edodes (Shiitake mushroom)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 362420.37

構造登録者

Gong, W.M.,Yang, L.Y. (登録日: 2019-01-26, 公開日: 2020-02-12, 最終更新日: 2024-11-13)

主引用文献

Yang, L.Y.,Chen, T.J.,Wang, F.,Li, L.,Yu, W.B.,Si, Y.K.,Chen, J.J.,Liu, W.C.,Zhu, P.,Gong, W.M.
Structures of beta-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition.
Commun Biol, 3:22-22, 2020

PubMed Abstract: LXYL-P1-2 is one of the few xylosidases that efficiently catalyze the reaction from 7-β-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT), and is a potential enzyme used in Taxol industrial production. Here we report the crystal structure of LXYL-P1-2 and its XDT binding complex. These structures reveal an enzyme/product complex with the sugar conformation different from the enzyme/substrate complex reported previously in GH3 enzymes, even in the whole glycohydrolases family. In addition, the DT binding pocket is identified as the structural basis for the substrate specificity. Further structure analysis reveals common features in LXYL-P1-2 and Taxol binding protein tubulin, which might provide useful information for designing new Taxol carrier proteins for drug delivery.

PubMed: 31925310
DOI: 10.1038/s42003-019-0744-4

実験手法

X-RAY DIFFRACTION (2.4 Å)