3ahz | pdb_00003ahz

Crystal structure of beta-glucosidase from termite Neotermes koshunensis in complex with Tris

spinqualitylabelsall models 3ahz, resolution 1.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ahz is a 1 chain structure with sequence from Neotermes koshunensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.34Å Ligands: GOL, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8T0W7_9NEOP 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 beta-Glucosidases (EC 3.2.1.21) cleave beta-glucosidic linkages in disaccharide or glucose-substituted molecules and play important roles in fundamental biological processes. beta-Glucosidases have been widely used in agricultural, biotechnological, industrial and medical applications. In this study, a high yield expression (70-250mg/l) in Escherichia coli of the three functional beta-glucosidase genes was obtained from the bacterium Clostridium cellulovorans (CcBglA), the fungus Trichoderma reesei (TrBgl2), and the termite Neotermes koshunensis (NkBgl) with the crystal structures of CcBglA, TrBgl2 and NkBgl, determined at 1.9A, 1.63A and 1.34A resolution, respectively. The overall structures of these enzymes are similar to those belonging to the beta-retaining glycosyl hydrolase family 1, which have a classical (alpha/beta)(8)-TIM barrel fold. Each contains a slot-like active site cleft and a more variable outer opening, related to its function in processing different lengths of beta-1,4-linked glucose derivatives. The two essential glutamate residues for hydrolysis are spatially conserved in the active site. In both TrBgl2 and NkBgl structures, a Tris molecule was found to bind at the active site, explaining the slight inhibition of hydrolase activity observed in Tris buffer. Manganese ions at 10mM exerted an approximate 2-fold enzyme activity enhancement of all three beta-glucosidases, with CcBglA catalyzing the most efficiently in hydrolysis reaction and tolerating Tris as well as some metal inhibition. In summary, our results for the structural and functional properties of these three beta-glucosidases from various biological sources open important avenues of exploration for further practical applications. Structural and functional analysis of three beta-glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis.,Jeng WY, Wang NC, Lin MH, Lin CT, Liaw YC, Chang WJ, Liu CI, Liang PH, Wang AH J Struct Biol. 2010 Aug 1. PMID:20682343 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase 3D structures

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