2.7.7.3: pantetheine-phosphate adenylyltransferase
This is an abbreviated version!
For detailed information about pantetheine-phosphate adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.3
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2.7.7.3
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ppats
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penultimate
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dpcoa
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pantothen
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pyrophosphate
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hexameric
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3\'-dephospho-coa
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nucleotidyltransferase
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dephosphocoenzyme
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phosphopantothenoylcysteine
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medicine
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drug development
- 2.7.7.3
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ppats
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penultimate
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dpcoa
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pantothen
- pyrophosphate
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hexameric
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3\'-dephospho-coa
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nucleotidyltransferase
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dephosphocoenzyme
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phosphopantothenoylcysteine
- medicine
- drug development
Reaction
Synonyms
3'-dephospho-CoA pyrophosphorylase, 4'-phosphopantetheine adenylyltransferase, 4-phosphopantetheine adenylyltransferase, CoaD, dephospho-CoA pyrophosphorylase, dephospho-coenzyme A pyrophosphorylase, Enterococcus faecalis PPAT, More, pantetheine phosphate adenylyltransferase, phosphopantetheine adenylyltransferase, PPAT
ECTree
2.7.7.3 pantetheine-phosphate adenylyltransferaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
in complex with sodium citrate, to 1.76 A resolution. Citrate binds at the ATP binding site
structures in complex with dephospho coenzyme A and coenzyme A, to 1.96 and 2.04 A resolution, respectively. Both bind in the substrate binding site
sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M sodium acetate pH 4.6, 30% (w/v) PEG 2000
ligand-unbound state and in complex with ATP and pantetheine, using 3.5 M sodium formate and 100 mM Tris-HCl (pH 8.5)
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The best crystals are grown with a reservoir solution consisting of 0.1 M sodium HEPES pH 7.5, 0.8 M sodium dihydrogen phosphate, and 0.8 M potassium dihydrogen phosphate. Tetragonal bipyramidal crystals grew to approximate dimensions of 0.1 x 0.1 x 0.1 mm within a few days.
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at pH 5.0, 100 mM sodium acetate, pH 5.0, 1.1 M ammonium sulfate, 200 mM NaCl
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co-crystallization with CoA, space group: I23, with a dimer in the asymmetric unit, a solvent content of 0.57 and a volume-to-protein mass ratio of 288 A3 Da-1
co-crystallization with inhibitor PTX040334 in 5% DMSO, 22-32% polyethylene glycol 8000, 200 mM ammonium sulfate in 100 mM cacodylate buffer, pH 6-6.5 at 21°C
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co-crystallization with pantetheine 4'-phosphate or ATP, space group: I23, with a dimer in the asymmetric unit, a solvent content of 57% and a volume-to-protein mass ratio of 288 A3 Da-1
hanging drop vapor diffusion method, using 0.1 M TrisHCl, pH 7.0, containing 2.0 M (NH4)2SO4 and 0.2 M Li2SO4
hanging-drop vapour-diffusion method, using sodium chloride as precipitant, trigonal space group P3121 or P3221 with six monomers in the asymmetric unit, a solvent content of 49% and a volume-to-protein mass ratio of 2.39 A3 Da-1
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apo form and in complex with ATP, counter-diffusion method, using 40 mM cacodylate buffer pH 5.5 containing 10 mM MgCl2, 0.15 mM NaCl, 20 mM cobalt hexamine and 15% (w/v) 2-methyl-2,4-pentanediol as precipitant solution
enzyme crystals are grown in microgravity by the capillary counter-diffusion method through a gel layer, mixing of 10 mg/ml protein in 10 mM HEPES, pH 8.0, 0.15 M NaCl, and 14 mM ATP, with reservoir solution containing 0.1 M NaAc, pH 5.0, 10 mM MgCl2, 5 mM HEPES, pH 8.0, 0.075 M NaCl, 14 mM ATP, and 1.1 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement method
enzyme in complex with pantetheine 4'-phosphate and adenosine-5'-[(alpha,beta)-methyleno]triphosphate, sitting drop vapor diffusion method, using 38% (v/v) polyethylene glycol 200 and 0.1 M HEPES (pH 7.2), at 21°C
in complex with coenzyme A, hanging drop vapor diffusion method, using 0.1 M Tris base pH 8.0 and 0.15 M magnesium formate
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space groups R32 and S32 using using 2-methyl-2,4-pentanediol or ammonium sulfate as the precipitant, respectively. Enzyme molecules in the crystals with space group P32 are more closely packed, and the access to the active site of the enzyme is restricted by intermolecular contacts. The independent hexameric molecule in the crystals with space group P32 forms a larger number of intermolecular polar contacts
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purified recombinant His-tagged enzyme in complex with diphosphate, substrate analogue AMPPNP, and inhibitors acetyl-CoA and CoA, sitting drop vapor diffusion method, mixing of 0.002 ml of protein in 25 mM HEPES, pH 7.0, 300 mM NaCl, and 2% glycerol, with 0.002 ml of well solution containing 17-19% PEG 4000, 0.1 M HEPES, pH 6.8-7.2, 200-350 mM Na-acetate, and 5-7% 2-propanol, 3-4 weeks, 42°C, method optimization, crystals are soaked in 0.1 mM ligand solution, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
structure of apo-PPAT. Residues R90 and D94 residues act like a gate near the binding cavity to accommodate and stabilize the incoming ligand
enzyme from Staphylococcus aureus subsp. aureus MW2 in complex with inhibitors, vapour diffusion method, mixing of 0.0025 ml of protein solution with 0.0025 ml of reservoir solution containing 14% to 19% PEG 3350, 200 mM ammonium sulfate, and 0.1 M propionic acid cacodylate Bis-Tris propane buffer, pH 7.5, 20°C, 5-7 days, X-ray diffraction structure determination and analysis at 1.72-2.38 A resolution, molecular replacement and modelling of inhibitor binding
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