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2.7.2.3: phosphoglycerate kinase

This is an abbreviated version!
For detailed information about phosphoglycerate kinase, go to the full flat file.

Word Map on EC 2.7.2.3

Reaction

ATP
+
3-phospho-D-glycerate
=
ADP
 +
3-phospho-D-glyceroyl phosphate

Synonyms

3-PGK, 3-phosphoglycerate 1-phosphotransferase, 3-phosphoglycerate kinase, 3-phosphoglycerate phosphokinase, 3-phosphoglyceric acid kinase, 3-phosphoglyceric acid phosphokinase, 3-phosphoglyceric kinase, AbPGK, ATP-3-phospho-D-glycerate-1-phosphotransferase, ATP:3-phospho-D-glycerate 1-phosphotransferase, ATP:D-3-phosphoglycerate 1-phosphotransferase, chl-PGK, glycerate 3-phosphate kinase, glycerophosphate kinase, HacPGK1, HacPGK2, HapPGK, hPGK, HsPGK, human 3-phosphoglycerate kinase, kinase (phosphorylating), phosphoglycerate, Mfer_0156, OsPGK2, P-glycerate kinase, PAS-PGK, PfPGK, PGK, PGK 1, PGK-1, PGK-2, pgk-B, PGK1, PGK2, Pgk3, Pgk5, PGKA, PGKase-1, PGKB, PGKC, pgkp1, pgkp2, phosphoglycerate kinase, phosphoglycerate kinase 1, phosphoglycerate kinase 2, phosphoglycerate kinase B, phosphoglycerate kinase-1, phosphoglyceric acid kinase, phosphoglyceric kinase, phosphoglycerokinase, PwPGK, SjPGK, SSO0527, testis-specific phosphoglycerate kinase 2, TRSC58_02767, X chromosome-linked phosphoglycerate kinase-1

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.2 Phosphotransferases with a carboxy group as acceptor
                2.7.2.3 phosphoglycerate kinase

Crystallization

Crystallization on EC 2.7.2.3 - phosphoglycerate kinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized using lithium sulfate as the precipitant to a resolution of 2.5 A. The AbPGK crystals belong to space group P2221
-
crystallization from ammonium sulfate precipitation
-
in the presence of 1 mM AMP-PNP and 1 mM MgCl2, by the vapor diffusion method, solved by molecular replacement to 2.4 A resolution
vapor diffusion method
hanging drop vapour phase diffusion method, 18°C, protein solution: 15 mg/ml, Tris-HCl, pH 7.0, 1 mM MgATP2-, 0.1 mM NaN3, 10% w/v polyethylene glycol 600, precipitant is 40% w/v polyethylene glycol 600, X-ray diffraction structure determination and analysis
-
crystallization from ammonium sulfate precipitate within 10 min, recrystallization
-
crystallization via precipitation with ammonium sulfate stepwise from 30-35% to 65% w/v within 24 h
-
crystallization via precipitation with ammonium sulfate stepwise from 60% to 75% w/v at room temperature for 2 h, then 4°C, several days
-
crystals of the 3PG-HsPGK binary complex in an open conformation (HsPGK-3PG-open) are grown, and ADP and the nonhydrolyzable ATP analogue, AMP-PCP, are introduced, by soaking, to investigate the effect of their binding on the open conformation
hPGK crystals are obtained at 20 °C by the sitting drop method. A crystal structure of hPGK in a fully closed conformation in complex with L-ADP, 3-phosphoglycerate, and the transition-state analogue AlF4- is determined
mutant enzymes V216F, G166D, M189I, and R38M, hanging drop vapor diffusion method
vapour diffusion in hanging drop method. Crystal structures of hPGK in its free state, or bound to L-ADP, D-ADP, D-CDP or L-CDP
crystallized in three forms: as the apoenzyme, as a complex with 3-phosphoglycerate, and as a complex with 3-phosphoglycerate and ATP. The crystal structures are solved to 2.7, 2.0, and 2.7 A resolutions, respectively
crystal structures of Plasmodium falciparum phosphoglycerate kinase (PfPGK) is determined in open conformation in two different crystal forms to 2.7 A and 3 A resolution, respectively. In both structures a sulfate ion is bound in the ATP binding site and a second sulfate ion is located at the regulatory basic patch in the second crystal form
hanging-drop vapour-diffusion method, recombinant enzyme forms a hexagonal space group P6(1)22 with unit cell parameters a = b = 140.7 A, c = 263.9 A, 3.0 A resolution
-
crystallization as native enzyme within 8-12 months or in complex with 3-phosphoglycerate and ATP analogue inhibitor beta,gamma-imido-adenosine-5'-triphosphate within 2-3 days, X-ray diffraction structure determination and analysis
hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol 4000, 0.2 M MgCl2 and 0.1 M Tris-HCl at pH 8.4
Pseudomonas sp. TACII 18
crystallization from ammonium sulfate precipitation, pH 7.0, room temperature, a few days, X-ray structure determination, in presence of 1% 1,4-dioxane and 68% ammonium sulfate, and analysis
-
enzyme in ternary complex with Mg2+-bound ATP analogue inhibitors Mg-beta,gamma-methylene-adenosine-5'-triphosphate and Mg-beta,gamma-imido-adenosine-5'-triphosphate, and substrate 3-phospho-D-glycerate, hanging drop vapour diffusion method, reservoir solution: 10 mM beta,gamma-methylene-adenosine-5'-triphosphate, 12 mM MgCl2, 10 mM 3-phospho-D-glycerate, 27-28% w/w polyethylene glycol 8000, pH 7.0, 15°C, a few weeks, X-ray structure determination and analysis
enzyme in ternary complex with MgADP and 3-phospho-D-glycerate, X-ray structure determination and analysis of the open and closed conformation during substrate binding
single crystals of the binary complexes with ATP (at 1.9 A resolution) and MgATP2- (at 2.1 A resolution) are grown in hanging drops, at 15°C, within about 2 weeks
-
crystal structure of unliganded PGK, solved by molecular replacement to 1.8 A resolution, crystals belong to the P212121 space group with one molecule per asymmetric unit
hanging drop vapour-diffusion method, enzyme crystallizes in the P2(1)2(1)2(1) space group with one molecule in the asymmetric unit, cell dimension a = 65.1, b = 71.3, c = 80.2 A, up to 1.8 A resolution
-
crystallization from ammonium sulfate precipitation overnight with gradually raising of temperature from 4°C to room temperature, in presence of ATP
-
crystallization from ammonium sulfate precipitation with 37% w/v by hanging or sitting drop vapour diffusion method, protein solution: 4 mg/ml, PIPES buffer, pH 6.8, 10 mM MgCl2, 1 mM ATP, 10% (NH4)2SO4, 22°C, 7-14 days, high resolution X-ray diffraction structure determination and analysis, rotating camera system
-
purified, recombinant enzyme is crystallized as a ternary complex by vapour diffusion method, 10°C, protein solution: 6 mg/ml, 10 mM 3-phospho-D-glycerate, 10 mM MgADP, 25 mM Tris, pH 7.5, 50 mM NaCl, 10 m DTT, plus equal volume of 2.5 M sodium potassium phosphate, pH 8.0
-
purified, recombinant enzyme is crystallized in complex with nucleotide analogue Mg-beta,gamma-imido-adenosine-5'-triphosphate by vapour diffusion method, 10°C, protein solution: 6 mg/ml, 10 mM 3-phospho-D-glycerate, 10 mM MgADP-, 25 mM Tris, pH 7.5, 50 mM NaCl, 10 m DTT, plus equal volume of 2.5 M sodium potassium phosphate, pH 7.5
-
structure determination and analysis
-
vapour diffusion method, protein solution containing 2.5 M potassium sodium phosphate, pH 8.0, X-ray diffraction structure determination and analysis
-