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Results 1 - 8 of 8
EC Number Crystallization (Commentary)
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70-
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70at a resolution of 2.8 A, TreX crystallized in the dimeric and tetrameric forms, in space groups P3121 and P321, respectively and in complex with an acarbose ligand. Acarbose intermediate is covalently bound to Asp363, occupying subsites -1 to -3
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70by hanging drop vapour-diffusion method, using polyethylene glycol 6000 as precipitant
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70crystal structures of DGase in uncomplexed form and a mutant in complex with isomaltotriose, to 2.2 A resolution, by the hanging-drop, vapor-diffusion method at 20°C. The enzyme is composed of three domains, A, B and C, and has a (beta/alpha)8-barrel in domain A. Three catalytic residues are located at the bottom of the active site pocket and the bound isomaltotriose occupies subsites -1 to +2. Hydrogen bonds between Asp60 and Arg398 and O4 atom of the glucose unit at subsite -1 accomplish recognition of the non-reducing end of the bound substrate. The side-chain atoms of Glu371 and Lys275 form hydrogen bonds with the O2 and O3 atoms of the glucose residue at subsite +1
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70determination of the structure of glucodextranase and of the complex of glucodextranase with acarbose at 2.42 A resolution
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70purified recombinant His-tagged enzyme, sitting drop vapour diffusion method, mixing of 16 mg/ml protein in 20 mM MES-NaOH, pH 6.5, 100 mM NaCl, and 2 mM CaCl2, with reservoir solution containing 20% glycerol, 16% PEG 8000, and 0.1 M MES, pH 6.5, in a 2:1 ratio, room temperature, X-ray diffraction structure determination and analysis at 2.05 A resolution, molecular replacement and modelling
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70sitting drop vapor diffusion method. Mutant E236Q glucosyl-enzyme intermediate are obtained by co-crystallization with 5 mM alpha-D-glucosyl fluoride at 100 mM Tris-HCl (pH 7.5), 200 mM calcium chloride and 18% (w/v) polyethylene glycol (PEG) 6000. The ligand-free E236Q crystals are grown by using 100 mM sodium 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (pH 7.4), 200 mM calcium chloride and 18% (w/v) PEG 6000
Show all pathways known for 3.2.1.70Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.70unliganded form and in complex with acarbose
Results 1 - 8 of 8