Literature summary for 3.2.1.170 extracted from

Miyazaki, T.; Ichikawa, M.; Iino, H.; Nishikawa, A.; Tonozuka, T.
Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8 (2015), J. Struct. Biol., 190, 21-30 .

Search for more literature for 3.2.1.170

Cloned(Commentary)

Cloned (Comment)	Organism
gene Tt8MGH, recombinant expression in Escherichia coli strain BL21 (DE3)	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Thermus thermophilus

Crystallization (Comment)

Organism

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

Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
125400	-	recombinant enzyme, gel filtration	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q5SJN0	-	-
Thermus thermophilus ATCC 27634	Q5SJN0	-	-
Thermus thermophilus DSM 579	Q5SJN0	-	-

Purification (Commentary)

Purification (Comment)	Organism
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	Thermus thermophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	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	Thermus thermophilus	?	-	?
additional information	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	Thermus thermophilus DSM 579	?	-	?
additional information	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	Thermus thermophilus ATCC 27634	?	-	?

Subunits

Subunits	Comment	Organism
homotrimer	3 * 48800, about, sequence calculation	Thermus thermophilus
More	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	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
GH63 mannosylglycerate hydrolase	-	Thermus thermophilus
Tt8MGH	-	Thermus thermophilus

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the glycosyl hydrolase family 63, GH 63	Thermus thermophilus