5BX4
Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with Glucoimidazole
Summary for 5BX4
| Entry DOI | 10.2210/pdb5bx4/pdb |
| Related | 5BVU 5BX2 5BX3 5BX5 |
| Descriptor | beta-glucosidase, GLUCOIMIDAZOLE, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | thermoanaerobacterium xylolyticum, gh116, beta-glucosidase, glucoimidazole, hydrolase |
| Biological source | Thermoanaerobacterium xylanolyticum LX-11 |
| Total number of polymer chains | 1 |
| Total formula weight | 93663.12 |
| Authors | Charoenwattanasatien, R.,Pengthaisong, S.,Sansenya, S.,Mutoh, R.,Tankrathok, A.,Tanaka, H.,Kurisu, G.,Ketudat Cairns, J.R. (deposition date: 2015-06-08, release date: 2016-05-18, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 27115290DOI: 10.1021/acschembio.6b00192 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report
