Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli strain BL21 (DE3) | 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | dependent on | Thermus thermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q72K29 | - |
- |
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | Q72K29 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21 (DE3) by cation exchange chromatography | Thermus thermophilus |
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 |
Subunits | Comment | Organism |
---|---|---|
More | detailed structure analysis, overview | Thermus thermophilus |
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 | 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 |