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6.3.5.3: phosphoribosylformylglycinamidine synthase

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

Word Map on EC 6.3.5.3

Reaction

ATP
+
N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
 +
L-glutamine
 +
H2O
=
ADP
 +
phosphate
 +
2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine
 +
L-glutamate

Synonyms

2-Formamido-N-ribosylacetamide 5'-phosphate:L-glutamine amido-ligase (adenosine diphosphate), 5'-phosphoribosylformyl glycinamidine synthetase, FGAM, FGAM synthase, FGAM synthetase, FGAM-synthetase, FGAMS, FGAR amidotransferase, FGAR-AT, FGARAT, formylglycinamide ribonucleotide amidotransferase, formylglycinamide ribonucleotide amidotransferase complex, Formylglycinamide ribonucloetide amidotransferase, Formylglycinamide ribotide amidotransferase, Formylglycinamide ribotide synthetase, formylglycinamide synthetase, LT2, mPurL, ORF75c, PFAS, phosphoribosylformylglycinamidine synthase II, Phosphoribosylformylglycinamidine synthetase, Phosphoribosylformylglycineamidine synthetase, Pur4, PurL, PurS, smPurL, StPurL, Synthetase, phosphoribosylformylglycinamide, TmPurL

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor
                6.3.5.3 phosphoribosylformylglycinamidine synthase

Crystallization

Crystallization on EC 6.3.5.3 - phosphoribosylformylglycinamidine synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of structure of PurS in two different crystal forms P2(1) and C2 at 2.5 and 2.0 A resolution, respectively. PurS forms a tight dimer with a central six-stranded beta-sheet flanked by four helices. In both the P2(1) and the C2 crystal forms, the quaternary structure of PurS is a tetramer. Native PurS is crystallized from 2.0 M ammonium sulfate, 6% PEG 400, 100 mM HEPES, pH 7.3. The crystals are grown at room temperature using the hanging-drop vapor diffusion technique. Drops containing a 2:1 mixture of protein and reservoir solution are optimal for crystal growth. Crystals grow over a period of 4-7 days. Under these conditions, PurS crystallizes in the monoclinic space group P2(1) with unit cell dimensions a = 42.91 A, b = 87.96 A, c = 52.68 A, and beta = 94.97°. The SeMet-PurS crystals grow in 20% PEG 4K, 5% glycerol, 15% 2-propanol, 100 mM sodium citrate, pH 5.6. Optimal drop size is 0.004 mL using a 1:1 mixture of protein and reservoir. Under these conditions, the protein crystallizes in the space group C2 with unit cell dimensions a = 89.13 A, b = 42.21 A, c = 47.03 A, and beta = 118.22°
-
to 2.3 A resolution. Molecular dynamics simulation and comparison with PurS from Thermus thermophilus and Methanocaldococcus jannaschii
crucial component MTH169, space group P4(3)22, unit cell parameters a : 53.8 A, c : 142.7 A
-
algorithm RismPath which enables fast and accurate determination of solvent distribution inside a protein channel, predicts an auxiliary ADP-adjacent path as the preferred mode of ammonia transfer. The residues in the middle of the channel do not partake in catalytic coupling and serve only as channel walls facilitating ammonia transfer
crystals of the pure SeMet-enzyme are grown at room temperature using hanging-drop vapor diffusion method. StPurL crystallizes in the hexagonal space group P6(5) with unit cell dimensions of a = 145.3 and c = 140.9 A. The asymmetric unit contains one monomer, corresponding to calculated solvent content of 57%. Domain organization revealed by X-ray crystallography
-
mutants R1263A and F209W, vapor diffusion method
to 1.55 A resolution. Molecular dynamics simulation and comparison with PurS from Thermus thermophilus and Methanocaldococcus jannaschii
crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) at 1.90 A resolution
hanging drop method, enzyme in complex with formylglycinamide ribonucleotide, mutant enzyme H72A in complex with beta,gamma-methylene adenosine 5'-triphosphate, mutant enzyme H72A in complex with ADP, enzyme in complex with formylglycinamide ribonucleotide and beta,gamma-methylene adenosine 5'-triphosphate, enzyme in complex with ATP
in complex with gene products PurQ and PurS, to 3.5 A resolution. The complex has a stoichiometry of 2:1:1 for components PurS:PurQ:PurL, respectively. The flexibility of the PurS dimer is involved in the activation of the complex and the formation of an ammonia channel
nanodroplet vapor diffusion method, crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 A resolution
to 1.64 A resolution. Molecular dynamics simulation and comparison with PurS from Sulfolobus tokodaii and Methanocaldococcus jannaschii