7e5j | pdb_00007e5j

Crystal structure of beta-glucosidase from Thermoanaerobacterium saccharolyticum

spinqualitylabelsall models 7e5j, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7e5j is a 1 chain structure with sequence from Thermoanaerobacterium saccharolyticum JW/SL-YS485. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.71Å Ligands: NA, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I3VXG7_THESW Publication Abstract from PubMed beta-Glucosidases (Bgls) convert cellobiose and other soluble cello-oligomers into glucose and play important roles in fundamental biological processes, providing energy sources in living organisms. Bgls are essential terminal enzymes of cellulose degradation systems and attractive targets for lignocellulose-based biotechnological applications. Characterization of novel Bgls is important for broadening our knowledge of this enzyme class and can provide insights into its further applications. In this study, we report the biochemical and structural analysis of a Bgl from the hemicellulose-degrading thermophilic anaerobe Thermoanaerobacterium saccharolyticum (TsaBgl). TsaBgl exhibited its maximum hydrolase activity on p-nitrophenyl-beta-d-glucopyranoside at pH 6.0 and 55 degrees C. The crystal structure of TsaBgl showed a single (beta/alpha)8 TIM-barrel fold, and a beta8-alpha14 loop, which is located around the substrate-binding pocket entrance, showing a unique conformation compared with other structurally known Bgls. A Tris molecule inhibited enzyme activity and was bound to the active site of TsaBgl coordinated by the catalytic residues Glu163 (proton donor) and Glu351 (nucleophile). Titration experiments showed that TsaBgl belongs to the glucose-tolerant Bgl family. The gatekeeper site of TsaBgl is similar to those of other glucose-tolerant Bgls, whereas Trp323 and Leu170, which are involved in glucose tolerance, show a unique configuration. Our results therefore improve our knowledge about the Tris-mediated inhibition and glucose tolerance of Bgl family members, which is essential for their industrial application. Biochemical and Structural Analysis of a Glucose-Tolerant beta-Glucosidase from the Hemicellulose-Degrading Thermoanaerobacterium saccharolyticum.,Kim IJ, Bornscheuer UT, Nam KH Molecules. 2022 Jan 4;27(1). pii: molecules27010290. doi:, 10.3390/molecules27010290. PMID:35011521 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase 3D structures

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