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5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent)

This is an abbreviated version!
For detailed information about phosphoglycerate mutase (2,3-diphosphoglycerate-independent), go to the full flat file.

Word Map on EC 5.4.2.12

Reaction

2-phospho-D-glycerate
=
3-phospho-D-glycerate

Synonyms

2,3-biphosphoglycerate-independent phosphoglycerate mutase, 2,3-diphosphoglycerate-independent phosphoglycerate mutase, 2,3BPG-independent PGAM, 3-phosphoglycerate mutase, apgM, co-factor-independent phosphoglycerate mutase, cofactor independent phosphoglycerate mutase, cofactor-independent phosphoglycerate mutase, cofactor-independent phosphoglycerate mutase 1, EC 2.7.5.3, EC 5.4.2.1, independent PGAM, independent PGM, iPGAM, iPGM, MJ0010, MJ1612, PGAM, PGM, PH0037, SSO0417

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.2 Phosphotransferases (phosphomutases)
                5.4.2.12 phosphoglycerate mutase (2,3-diphosphoglycerate-independent)

Crystallization

Crystallization on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein is composed of two structural and functiional domains, the phosphatase and the transferase. Comparison with the structurally similar domains of in Bacillus stearothermophilus
crystals of iPGM complexed with 3-phosphoglycerate and Mn2+ at 1.9 A resolution
crystals of wild-type and S62A mutant at 1.4 A resolution
-
methionyl and selenomethionyl phosphoglycerate mutase, vapor drop hanging diffusion, mixing equal volumes of protein solution, i.e. 50 mg/ml protein in 150 mM 3-phosphoglycerate, pH 7.4 and reservoir solution containing 2 M ammonium sulfate, 25 mM zinc acetate, 20 mM cesium chloride, 15 mM 2-mercaptoethanol, 3% polyethylene glycol 200 and 50 mM Tris-HCl, pH 7.4, crystals diffract to 2.5 A resolution
crystals of iPGAM complexed with 3-phosphoglycerate and Co2+, hanging-drop vapor diffusion, crystallization drops contain equal volumes of reservoir and enzyme solution, 5 mg/ml iPGAM, 1.5 mM 3-phosphoglycerate, 50 mM NaCl, 0.01 mM CoCl2 in 20 mM TEA buffer, pH 7.4, crystals diffract to 1.9 A
iPGAM crystallized with 3-phosphoglycerate or 2-phosphoglycerate at high and low cobalt concentrations (4 mM and 0.01 mM), hanging drop vapor diffusion method, using 0.08 M ammonium acetate, 0.04 M trisodium citrate dihydrate pH 6.0, and 24% (w/v) PEG 4000
space group R32, resolution of 2.2 A
-
hanging drop vapor diffusion method, using 0.2 M NaCl, 0.1 M Bis/Tris pH 6.3 and 25% (w/v) polyethylene glycol 3350
sitting drop vapor diffusion method, using either 0.1 M HEPES pH 7.5, 20% (w/v) polyethylene glycol 10000 or 0.2 M NaCl, 0.1 M bis-Tris pH 6.5, 25% (w/v) polyethylene glycol 3350, at 25°C
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.003 ml of 8 mg/ml protein solution containing 20 mM Tris-acetate-EDTA, pH 7.4, 50 mM NaCl, 001 mM CoCl2, with 0.003 ml of reservoir solution containing 0.05 M ammonium sulfate, 0.1 M Bis-Tris, pH 6.1, and 25% w/v PEG 3350, 18°C, X-ray diffraction structure determination and analysis at 2.3 A resolution