1W2T
beta-fructosidase from Thermotoga maritima in complex with raffinose
Summary for 1W2T
| Entry DOI | 10.2210/pdb1w2t/pdb |
| Related | 1UYP |
| Descriptor | BETA FRUCTOSIDASE, beta-D-fructofuranose-(2-1)-[alpha-D-galactopyranose-(1-6)]alpha-D-glucopyranose, CITRIC ACID, ... (5 entities in total) |
| Functional Keywords | hydrolase, glycosidase, invertase, raffinose, beta fructosidase |
| Biological source | THERMOTOGA MARITIMA |
| Total number of polymer chains | 6 |
| Total formula weight | 302836.01 |
| Authors | Alberto, F.,Henrissat, B.,Czjzek, M. (deposition date: 2004-07-08, release date: 2005-10-26, Last modification date: 2023-12-13) |
| Primary citation | Alberto, F.,Jordi, E.,Henrissat, B.,Czjzek, M. Crystal Structure of Inactivated Thermotoga Maritima Invertase in Complex with the Trisaccharide Substrate Raffinose. Biochem.J., 395:457-, 2006 Cited by PubMed Abstract: Thermotoga maritima invertase (beta-fructosidase), a member of the glycoside hydrolase family GH-32, readily releases beta-D-fructose from sucrose, raffinose and fructan polymers such as inulin. These carbohydrates represent major carbon and energy sources for prokaryotes and eukaryotes. The invertase cleaves beta-fructopyranosidic linkages by a double-displacement mechanism, which involves a nucleophilic aspartate and a catalytic glutamic acid acting as a general acid/base. The three-dimensional structure of invertase shows a bimodular enzyme with a five bladed beta-propeller catalytic domain linked to a beta-sandwich of unknown function. In the present study we report the crystal structure of the inactivated invertase in interaction with the natural substrate molecule alpha-D-galactopyranosyl-(1,6)-alpha-D-glucopyranosyl-beta-D-fructofuranoside (raffinose) at 1.87 A (1 A=0.1 nm) resolution. The structural analysis of the complex reveals the presence of three binding-subsites, which explains why T. maritima invertase exhibits a higher affinity for raffinose than sucrose, but a lower catalytic efficiency with raffinose as substrate than with sucrose. PubMed: 16411890DOI: 10.1042/BJ20051936 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
Download full validation report
