5BX5

Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with glucose

5BX5 の概要

• エントリーDOI: 10.2210/pdb5bx5/pdb
• 関連するPDBエントリー: 5BVU 5BX2 5BX3 5BX4
• 分子名称: beta-glucosidase, beta-D-glucopyranose, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: thermoanaerobacterium xylanolyticum lx-11, gh116, beta-glucosidase, glucose, hydrolase
• 由来する生物種: Thermoanaerobacterium xylanolyticum LX-11
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 93089.52

構造登録者

Charoenwattanasatien, R.,Pengthaisong, S.,Sansenya, S.,Mutoh, R.,Hua, Y.,Tanaka, H.,Kurisu, G.,Ketudat Cairns, J.R. (登録日: 2015-06-08, 公開日: 2016-05-18, 最終更新日: 2023-11-08)

主引用文献

Charoenwattanasatien, R.,Pengthaisong, S.,Breen, I.,Mutoh, R.,Sansenya, S.,Hua, Y.,Tankrathok, A.,Wu, L.,Songsiriritthigul, C.,Tanaka, H.,Williams, S.J.,Davies, G.J.,Kurisu, G.,Ketudat Cairns, J.R.
Bacterial beta-Glucosidase Reveals the Structural and Functional Basis of Genetic Defects in Human Glucocerebrosidase 2 (GBA2)
Acs Chem.Biol., 11:1891-1900, 2016

PubMed Abstract: Human glucosylcerebrosidase 2 (GBA2) of the CAZy family GH116 is responsible for the breakdown of glycosphingolipids on the cytoplasmic face of the endoplasmic reticulum and Golgi apparatus. Genetic defects in GBA2 result in spastic paraplegia and cerebellar ataxia, while cross-talk between GBA2 and GBA1 glucosylceramidases may affect Gaucher disease. Here, we report the first three-dimensional structure for any GH116 enzyme, Thermoanaerobacterium xylanolyticum TxGH116 β-glucosidase, alone and in complex with diverse ligands. These structures allow identification of the glucoside binding and active site residues, which are shown to be conserved with GBA2. Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2.

PubMed: 27115290
DOI: 10.1021/acschembio.6b00192

実験手法

X-RAY DIFFRACTION (1.85 Å)