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2.4.2.17: ATP phosphoribosyltransferase

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

Word Map on EC 2.4.2.17

Reaction

1-(5-phospho-beta-D-ribosyl)-ATP
+
diphosphate
=
ATP
 +
5-phospho-alpha-D-ribose 1-diphosphate

Synonyms

1-(5-phospho-D-ribosyl)-ATP:pyrophosphate phospho-alpha-D-ribosyltransferase, adenosine 5'-triphosphate phosphoribosyltransferase, adenosine triphosphate phosphoribosyltransferase, adenosine-triphosphate phosphoribosyltransferase, ATP phosphoribosyl transferase, ATP phosphoribosyl transferase complex, ATP phosphoribosyltransferase, ATP-phosphoribosyl transferase, ATP-phosphoribosyltransferase, ATP-PRT, ATP-PRT1, ATP-PRT2, ATP-PRTase, ATPPRT, HisG, HisGL, N-1-(5'-phosphoribosyl)-ATP transferase, phosphoribosyl ATP synthetase, phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase, phosphoribosyl-ATP pyrophosphorylase, phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase, phosphoribosyladenosine triphosphate pyrophosphorylase, phosphoribosyladenosine triphosphate synthetase, phosphoribosyltransferase, adenosine triphosphate

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.17 ATP phosphoribosyltransferase

Crystallization

Crystallization on EC 2.4.2.17 - ATP phosphoribosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ATP, L-histidine, or L-histidine/AMP, hanging drop vapor diffusion method, using 0.1M sodium acetate, 0.1 M MgCl2, 13-15% (w/v) PEG 4000, pH 5.5 (ATP), or 0.1 M BTP, 0.2 M KSCN, 13-14% (w/v) PEG 3350, pH 6.5 (His), or 0.1 M Tris, 0.1 M MgCl2, 13-15% (w/v) PEG 4000, pH 7.5 (L-His/AMP)
truncated long-form enzyme devoid of its regulatory domain as apoenzyme and in complex with ATP, 5-phospho-alpha-D-ribose 1-diphosphate or 1-(5-phospho-beta-D-ribosyl)-ATP, hanging drop vapor diffusion method, using 1 M sodium acetate, 10 mM ZnCl2, and 7-10% (w/v) PEG 6000 (pH 5.0)
purified recombinant selenomethionine-labeled enzyme in complex with inhibitor AMP or with product 1-(5-phospho-D-ribosyl)-ATP, X-ray diffraction enzyme-inhibitor complex structure determination and analysis at 2.7 A resolution, X-ray diffraction enzyme-product complex structure determination and analysis at 2.9 A resolution, modeling
vapour diffusion method, trigonal prisms are obtained using 1.3 M sodium tartrate, 50-200 mM magnesium chloride, 100 mM citrate buffer pH 5.6 and enzyme in the presence of 2 mM AMP, round shaped crystals are obtained with 1.36-1.44 M ammonium sulfate, 0-0.3 M sodium chloride, 100 mM HEPES buffer pH 7.5 and enzyme in the presence of 2 mM AMP
-
purified recombinant wild-type and selenomethionine-labeled enzyme complex, the latter additionally by microseeding, hanging drop vapour diffusion method, 0.002 ml well solution containing 15-25% v/v PEG 400, 0.1 M Tris-HCl, pH 7.5, 0.2 M MgCl2, mixed with equal volume of protein solution containing 10-16 mg/ml protein, 10 mM ATP, or 10 mM N-1-methyl-ATP and 5 mM 5-phospho-alpha-D-ribose 1-diphosphate, crystal growth is dependent on ATP or N-1-methyl-ATP, derivatization with 2.5 mM sodium tungstate dihydrate, cryoprotection with 17-18% glycerol, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution
-
native and SeMet-labeled enzyme, hanging drop vapor diffusion method, using 2.53 M NaCl, 100 mM Bis-Tris propane pH 6.3, and 10% (v/v) glycerol
hanging drop vapor diffusion method
hanging drop vapour diffusion method at 16°C, the apocrystals are obtained using 0.1 M buffer MES pH 6.5 and magnesium sulfate as precipitant, crystals in the presence of AMP and histidine are obtained using 0.1 M sodium citrate pH 5.6, 0.5 M ammonium sulfate and 1 M lithium sulfate with 5 mM AMP and 0.1 mM histidine
-
HisG co-crystallized with compound 6, to 2.9 A resolution
hanging drop vapor diffusion method, using 11% (w/v) PEG 3350, 0.1 M bicine (pH 8.5), 0.15 M SrCl2, 0.15 M KBr, and 2% (v/v) 1,6-hexanediol
holoenzyme and catalytic subunit HisGS in complexes with substrates (5-phospho-alpha-D-ribose 1-diphosphate, 5-phospho-alpha-D-ribose 1-diphosphate-ATP, 5-phospho-alpha-D-ribose 1-diphosphate-ADP), product (N1-(5-phospho-beta-D-ribosyl)-ATP) and inhibitor (AMP), hanging drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350, 0.1 M bicine pH 8.5, 50 mM MgCl2, 0.1 M KBr, and 4% (v/v) 1,6-hexanediol
purified recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ separately, in a binary complex with histidine, sitting drop vapour diffusion method, 0.002 ml of 8 mg/ml protein mixed with 0.002 ml reservoir solution containing 22.5% w/v methyl-2,4-pentanediol, 0.2 M phosphate/citrate buffer, pH 4.2, 2 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling
-