1w2t | pdb_00001w2t

beta-fructosidase from Thermotoga maritima in complex with raffinose

spinqualitylabelsall models 1w2t, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1w2t is a 6 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.87Å Ligands: CIT, FRU, GLA, GLC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BFRA_THEMA Hydrolysis of sucrose, raffinose, inulin and levan. Specific for the fructose moiety and the beta-anomeric configuration of the glycosidic linkages of its substrates. The enzyme released fructose from sucrose and raffinose, and the fructose polymer inulin is hydrolyzed quantitatively in an exo-type fashion. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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-fructofuranos ide (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. Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose.,Alberto F, Jordi E, Henrissat B, Czjzek M Biochem J. 2006 May 1;395(3):457-62. PMID:16411890 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Invertase

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