Literature summary for 3.1.3.70 extracted from

Goncalves, S.; Esteves, A.M.; Santos, H.; Borges, N.; Matias, P.M.
The three-dimensional structure of mannosyl-3-phosphoglycerate phosphatase from Thermus thermophilus HB27: a new member of the haloalkanoic acid dehalogenase superfamily (2011), Biochemistry, 50, 9551-9567.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli strain BL21 (DE3)	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme in apo-form and in complex with substrates, substrate analogues and inhibitors, sitting drop vapor diffusion technique, 10 mg/ml protein in 20 mM MES-NaOH pH 6.3, 760 mM NaCl, 5 mM DTT, 1 mM EDTA, 5 mM Mg2+ and Na/KPO4, is mixed with crystallization solution containing 0.02 M of each of the carboxylic acids, i.e. Na-formate, NH4-acetate, Na3-citrate, NaK-L-tartrate and Na-oxamate, 0.1 M MES/imidazole, pH 6.5, in a 1:1 molar ratio, and a 30% v/v precipitant mixture containing 20% v/v ethylene glycol and 10% v/v PEG 8000, 20°C, 5 days, X-ray diffraction structure determination and analysis, molecular replacement	Thermus thermophilus

Crystallization (Comment)

Organism

purified recombinant enzyme in apo-form and in complex with substrates, substrate analogues and inhibitors, sitting drop vapor diffusion technique, 10 mg/ml protein in 20 mM MES-NaOH pH 6.3, 760 mM NaCl, 5 mM DTT, 1 mM EDTA, 5 mM Mg2+ and Na/KPO4, is mixed with crystallization solution containing 0.02 M of each of the carboxylic acids, i.e. Na-formate, NH4-acetate, Na3-citrate, NaK-L-tartrate and Na-oxamate, 0.1 M MES/imidazole, pH 6.5, in a 1:1 molar ratio, and a 30% v/v precipitant mixture containing 20% v/v ethylene glycol and 10% v/v PEG 8000, 20°C, 5 days, X-ray diffraction structure determination and analysis, molecular replacement

Thermus thermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	dependent on	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q72K29	-	-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039	Q72K29	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain BL21 (DE3) by cation exchange chromatography	Thermus thermophilus

Reaction

Reaction	Comment	Organism	Reaction ID
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate	in Thermus thermophilus strain HB27 MpgP the phosphoryl-transfer undergoes a concerted DNSN mechanism with assistance of proton transfer from the general acid Asp8, forming a short-lived PO3- intermediate which is attacked by a nucleophilic water molecule, structure-activity relationship analysis, overview	Thermus thermophilus	a

Subunits

Subunits	Comment	Organism
More	detailed structure analysis, overview	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
More	the enzyme is a member of the haloalkanoic acid dehalogenase superfamily. It is a metal-dependent haloalcanoic acid dehalogenase-like phosphatase, preserving the catalytic Motifs I-IV of the HAD-core domain, and classified as a Cof-type MPGP based on its C2B cap insertion module	Thermus thermophilus
MPGP	-	Thermus thermophilus

General Information

General Information	Comment	Organism
metabolism	mannosyl-3-phosphoglycerate phosphatase is the enzyme involved in the second step of the two-step mannosyl-3-phosphoglycerate biosynthetic pathway, most commonly found in (hyper)thermophilic microorganisms	Thermus thermophilus
additional information	two distinct enzyme conformations, open and closed, are catalytically relevant: the apo-MpgP is prevalently found in the open state, while the holo-MpgP, in complex with the reaction products, is found in the closed state. Enzyme activation entails a structural rearrangement of Motifs I and IV with concomitant binding of the co-catalytic Mg2+ ion. The closure motion of the C2B domain is subsequently triggered by the anchoring of the phosphoryl group to the co-catalytic metal center, and by Arg167 fixing the mannosyl moiety inside the catalytic pocket	Thermus thermophilus
physiological function	mannosyl-3-phosphoglycerate phosphatase is a key mediator in the physiological response to thermal and osmotic stresses, catalyzing the hydrolysis of mannosyl-3-phosphoglycerate into the final product, alpha-mannosylglycerate	Thermus thermophilus