The enzyme occurs in thermophilic bacteria and has been characterized in Thermus thermophilus and Rubrobacter radiotolerans. It also has been identified in the moss Selaginella moellendorffii.
The enzyme appears in viruses and cellular organisms
The enzyme occurs in thermophilic bacteria and has been characterized in Thermus thermophilus and Rubrobacter radiotolerans. It also has been identified in the moss Selaginella moellendorffii.
Substrates: conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates, substrate recognition mechanism for GH63 mannosylglycerate hydrolase, overview Products: -
Substrates: conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates, substrate recognition mechanism for GH63 mannosylglycerate hydrolase, overview Products: -
Substrates: conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates, substrate recognition mechanism for GH63 mannosylglycerate hydrolase, overview Products: -
enzyme Tt8MGH consists of a single (alpha/alpha)6-barrel catalytic domain with two additional helices and two long loops which form a homotrimer, structure comparisons, overview. The conformations of three flexible loops are largely different from each other. The trimer is clover leaf-shaped
enzyme Tt8MGH consists of a single (alpha/alpha)6-barrel catalytic domain with two additional helices and two long loops which form a homotrimer, structure comparisons, overview. The conformations of three flexible loops are largely different from each other. The trimer is clover leaf-shaped
enzyme Tt8MGH consists of a single (alpha/alpha)6-barrel catalytic domain with two additional helices and two long loops which form a homotrimer, structure comparisons, overview. The conformations of three flexible loops are largely different from each other. The trimer is clover leaf-shaped
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme free or in complexes with glucose or glycerate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 10 mM Tris-HCl, pH 7.5, with 0.001 ml of reservoir solution containing 20-35% v/v 2-methyl-2,4-pentanediol and 100 mM Tris-HCl, pH 5.5-6.5, for co-crystallization with glucose or glycerate, the protein solution is mixed with 10 mM ligand solution, and stored at 4°C overnight. The Tt8MGH-Glc complex crystals are grown with the same method except that 100 mM sodium citrate buffer, pH 4.8-6.0, is used instead of Tris-HCl buffer in the reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.77-2.10 A resolution, molecular replacement method using PDB 2Z07 as a search model, modelling
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 (DE3) by heat treatment at 70°C for 10 min, followed by hydrophobic interaction and anion exchange chromatography, to homogeneity
Sampaio, M.; Chevance, F.; Dippel, R.; Eppler, T.; Schlegel, A.; Boos, W.; Lu, Y.; Rock, C.
Phosphotransferase-mediated transport of the osmolyte 2-O-alpha-mannosyl-D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA) gene and is regulated by the mngR (farR) gene product acting as repressor
J. Biol. Chem.
279
5537-5548
2004
Escherichia coli, Escherichia coli LYJ1, no activity in Escherichia coli, no activity in Escherichia coli LYJ2
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