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2.4.2.18: anthranilate phosphoribosyltransferase

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

Word Map on EC 2.4.2.18

Reaction

N-(5-phospho-D-ribosyl)-anthranilate
+
diphosphate
=
anthranilate
 +
5-phospho-alpha-D-ribose 1-diphosphate

Synonyms

AnPRT, anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyl transferase, anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyltransferase, anthranilate PRT, anthranilate-5-phosphoribosylphosphate phosphoribosyltransferase, anthranilate-PP-ribose-P phosphoribosyltransferase, More, Pat, phosphoribosyl-anthranilate pyrophosphorylase, phosphoribosylanthranilate pyrophosphorylase, phosphoribosylanthranilate transferase, phosphoribosyltransferase, anthranilate, PR transferase, PRT, sAnPRT, ssAnPRT, SSO0890, ssTrpD, strpD, Trp D, TrpD, TTC1491

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.18 anthranilate phosphoribosyltransferase

Crystallization

Crystallization on EC 2.4.2.18 - anthranilate phosphoribosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors, hanging drop vapor diffusion method, using 0.2 M imidazole. malate, pH 7.0, 15% (w/v) PEG 4000
mutant enzymes N138A, P180A, R193L, R193A, R194A, and G107P, hanging drop vapor diffusion method, using
hanging drop vapor diffusion method, complexed with Mn2+ diphosphate
-
crystal structures of the wild-type enzyme complexed to its two natural substrates anthranilate and 5-phosphoribosyl-1-pyrophosphate/Mg2+
hanging drop vapor diffusion method
hanging-drop method, crystals of ssTrpD diffract to better than 2.6 A resolution
mutant D83G/F149S in complex with 5-phospho-alpha-D-ribose 1-diphosphate and Mn2+, to 2.25 A resolution. Protein backbone of mutant D83G/F149S shows no detectable differences to the wild-type enzyme, whereas 5-phospho-alpha-D-ribose 1-diphosphate bound to mutant D83G/F149S adopts an extended conformation that contrasts markedly with the S compact shape observed in complexes of the wild-type enzyme
mutant M47D, structurally very similar to wild-type (rms deviation of 0.7 A for most of equivalent C(alpha) atoms) but reduced buried surface area per subunit compared to wild-type homodimer, Aps47 protonated at pH 6, crystals of space group P2 with four molecules (two homodimers) per asymmetric unit and A2 pseudo-symmetry, unit cell parameters a=91.6 A, b=65.9 A, c=115.7 A, beta=107.4°, 45% (v/v) solvent content, hanging drop method: 1 microlitre protein solution (5 mg/ml) + 1 microlitre reservior solution (50 mM MES pH 6.0, 18% (v/v) PEG, 5% (v/v) glycerol), room temperature, 72 h
the crystal structure of the dimeric class III phosphoribosyltransferase. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is coordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families
free enzyme and in the presence of Zn2+, hanging drop vapor diffusion method, using 0.2 M sodium acetate (pH 7.5), 20% (w/v) PEG 3350