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2.7.1.33: pantothenate kinase

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

Word Map on EC 2.7.1.33

Reaction

ATP
+
(R)-pantothenate
=
ADP
 +
(R)-4'-phosphopantothenate

Synonyms

4-phosphopantoate, BaPanK, Cab1, Cab1p, CoaA, coaW, CoaX, D-pantothenate kinase, EhPAnK, fumble, hPanK, hPanK1, hPANK2, hPanK3, hPanK4, HpPanK-III, HsPANK3, HsPANK4, kinase, pantothenate (phosphorylating), More, mPank, mPank1, mPanK2, mPanK3, MtCoaA, MtPanK, PAK, PanK, PanK-III, PanK1, PanK1alpha, PanK1b, PanK2, PanK3, PanK4, PanKBa, pantothenate kinase, pantothenate kinase 1, pantothenate kinase 2, pantothenate kinase 3, pantothenate kinase 4, pantothenate kinase-2, pantothenic acid kinase, PfPanK, Pfpank1, PoK, rPanK4, Rts protein , Rv1092c, TK2141, TmPanK-III, type II pantothenate kinase, type III pantothenate kinase

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.33 pantothenate kinase

Crystallization

Crystallization on EC 2.7.1.33 - pantothenate kinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method using 24-26% ethylene glycol
sitting-drop method. The crystal structure of Bacillus anthracis PanK is solved using multiwavelength anomalous dispersion data and refined at a resolution of 2.0 A
purified recombinant enzyme in a ternary complex with ADP and pantothenate, hanging drop vapour diffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 1 mM DTT, 1 mM EDTA, incubated overnight with 30 mM ADP, 30 mM pantothenate, and 30 mM magnesium nitrate, mixing in equal volumes with reservoir solution containing 11% PEG 3350, 0.2 M sodium citrate, pH 8.2, at 18°C, 1 week, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular modeling of N-alkylpantothenamides, growth-inhibitory anti-metabolites
sitting drop vapor diffusion method at 18°C, homodimeric structures of the catalytic core of PanK1alpha in complex with acetyl-CoA. Crystallographic mapping of missense mutations associated with pantothenate kinase-associated neurodegeneration disease
sitting drop vapor diffusion method at 18°C, homodimeric structures of the catalytic core of PanK3 in complex with acetyl-CoA. Crystallographic mapping of missense mutations associated with pantothenate kinase-associated neurodegeneration disease
in complex with N-pyridin-3-ylmethylpantothenamide, sitting drop vapor diffusion method, using 20% (w/v) PEG3350 and 0.2 M tri-lithium citrate
in complex with N-[2-(1,3-benzodioxol-5-yl)ethyl] pantothenamide, hanging drop vapor diffusion method, using 2 M sodium formate and 0.1 M Tris-HCl pH 8.5
bound to oantothenate, pantothenol or N-nonylpantothenamide, using 1.4-1.8 M trisodium citrate, 0.05-0.1 M sodium acetate and 10% (v/v) glycerol at pH 6.5
complexes of the enzyme with guanosine-5'-[(beta,gamma)-methyleno]triphosphate and pantothenate, GDP and phosphopantothenate, GDP, GDP and pantothenate, 5'-adenylyl (beta,gamma-methylene)diphosphonate, and guanosine-5'-[(beta,gamma)-methyleno]triphosphate, hanging drop vapor diffusion method, using 1.4-1.8 M trisodium citrate, 0.05-0.1 M sodium acetate, and 10% (v/v) glycerol at pH 6.5
-
hanging drop vapour diffusion method using 10-15% (w/v) PEG 8000, 0.05-0.1 M NaOAc and 0.05 M NaCl dissolved in 0.1 M sodium cacodylate buffer pH 6.5
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, 0.003 ml protein solution containing 6 mg/ml protein, 0.1 M Tris-HCl, pH 8.0, 0.15 M NaCl, 5% v/v glycerol and 0.001 M 2-mercaptoethanol, mixed 0.001 ml of precipitant solution containing 10-15% w/v PEG 8000, 0.05-0.1 M NaOAc, 0.05 NaCl, and 0.1 M cacodylate, pH 6.5, room temperature, equilibration against 0.4 ml precipitant solution, 3-7 days, 2 different crystal forms, X-ray diffraction structure determination and analysis at 2.5 A and 2.9 A resolution, respectively, molecular replacement calculations
-
purified recombinant His-tagged wild-type and mutant enzymes in apoform, microbatch-under-oil method, mixing of 0.002 ml of 6.5 mg/ml protein in 100 mM Tris-HCl, pH 7.8, 600 mM NaCl, 5% glycerol, and 100 mM imidazole, with 0.002 ml of precipitant solution that contains for mutant F247A: 0.2 M (NH4)2SO4, 0.1 M bis-Tris, pH 5.5, and 25% w/v PEG 3350, for mutant F254A: 10-15% w/v PEG 400, 1.25 M (NH4)2SO4, and 100 mM Na HEPES, pH 7.5, and for the double mutant F247A/F254A: 2% w/v PEG 400, 2.0 M (NH4)2SO4, and 100 mM Na HEPES, pH 7.5, at 22°C, X-ray diffraction structure determination and analysis at 1.80-3.20 A resolution, modeling
sitting drop vapor diffusion method, using 14.4% (w/v) PEG 8000, 20% (v/v) glycerol, 0.08 m sodium cacodylate, pH 6.5, and 0.16 m magnesium acetate
hanging drop vapour diffusion method using 28% (w/v) PEG 2000 mM and 0.1M Bis-Tris (pH 6.5), at 18°C
in complex with N-[2-(1,3-benzodioxol-5-yl)ethyl] pantothenamide, hanging drop vapor diffusion method, using 1.4 M sodium citrate, 0.1 M HEPES pH 7.5 and 5% (v/v) ethylene glycol
purified recombinant enzyme SaPanKII in complex with inhibitors N-pentylpantothenamide, N-heptylpantothenamide, N-(5-methoxypentyl)pantothenamide, and N-(benzo[d][1,3]dioxol-5-ylmethyl)pantothenamide, sitting drop vapor diffusion method, 500 nl of 20-30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 200 mM NaCl, and 10 mM dithiothreitol, and addition of 1.1% w/v cyclohexylethanoyl-N-hydroxyethylglucamide, ligand, and ATP, is mixed with 500 nl of well solution containing 25-35% PEG 4000, 0.2 M MgCl2, and 0.1 M Tris, pH 8.5, X-ray diffraction structure determination and analysis at 1.40-1.80 A resolution
A0A167Z3Z6
sitting drop vapour diffusion method using 28% (w/v) PEG 2 M and 0.1 M Bis-Tris (pH 6.5), at 18°C
hanging drop vapor-diffusion method, crystal structures of PanK-III in complex with pantothenate, phosphopantothenate as well as a ternary complex structure of PanK-III with pantothenate and ADP
sitting drop vapour diffusion method with 15% polyethylene glycol 3350
-