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2.4.2.29: tRNA-guanosine34 preQ1 transglycosylase

This is an abbreviated version!
For detailed information about tRNA-guanosine34 preQ1 transglycosylase, go to the full flat file.

Word Map on EC 2.4.2.29

Reaction

guanine34 in tRNA
+
7-aminomethyl-7-carbaguanine
=
7-aminomethyl-7-carbaguanine34 in tRNA
 +
guanine

Synonyms

ArcTGT, guanine insertion enzyme, guanine, queuine-tRNA transglycosylase, Q-insertase, QTRT1, QueTGT, queuine insertase, queuine tRNA ribosyltransferase, queuine tRNA-ribosyltransferase, queuine tRNA-ribosyltransferase subunit 1, ribosyltransferase, queuine transfer ribonucleate, TGT, transfer ribonucleate glycosyltransferase, tRNA guanine transglycosidase, tRNA guanine transglycosylase, tRNA transglycosylase, tRNA-guanine 34 transglycosylase, tRNA-guanine transglycosylase, tRNA–guanine transglycosylase, virulence-associated protein VACC

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.29 tRNA-guanosine34 preQ1 transglycosylase

Crystallization

Crystallization on EC 2.4.2.29 - tRNA-guanosine34 preQ1 transglycosylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with queuine, sitting or hanging drop vapor diffusion method, using 100 mM Tris pH 7.8, 200 mM KBr, 200 mM KSCN, 3% (w/v) polyglutamic acid-LM, 5% (w/v) PEG 4000
2-aminolin-benzoguanine inhibitors in complex with TGT, by hanging-drop, vapor diffusion method at 0°C and macro-seeding, to 1.28-1.78 A resolution, crystals belong to space group C2. The 2-amino-lin-benzoguanines are protonated upon binding to TGT. At pH 5.5, Asp102 is rotated to 75% into the guanine binding pocket whereas at pH 8.5 the same residue is oriented to 100% out of the pocket. Pronounced disorder of the attached side chains addressing the ribose 33 binding pocket
enzyme-inhibitor complexes with 3,5-diaminophthalhydrazide, 4-aminophthalhydrazide, 5-aminonaphthalene-2,3-hydrazide, 5-amino-3-(1H-[1,2,4]triazole-3-yl-sulfanyl)-phthalhydrazide, 5-amino-3-(5-amino-1H-[1,2,4]triazol-3-yl-sulfanyl)-phthalhydrazide. 1.95 A crystal structure of 4-aminophthalhydrazide in complex with the enzyme
in complex with guanine, pre-queuine 0, and pre-queuine 1, hanging drop vapour diffusion method, in 100 mM MES, pH 5.5, 1 mM dithiothreitol, 13% (w/v) PEG 8000, 10% (v/v) dimethyl sulfoxide
in complex with linbenzoguanine (6-aminoimidazol[4,5-g]quinazolin-8(7H)-one), hanging drop vapour diffusion method, in with 100 mM MES buffer (pH 5.5), 1 mM dithiothreitol, 8% (w/v) PEG 8000, 10% DMSO, at 20°C
mutant K52M, by hanging-drop, vapor-diffusion method and followed by macroseeding, at a resolution of 2.0 A, forms crystals under the same conditions as wild-type, while all attempts to obtain diffracting crystals from mutant Y330F are unsuccessful. Compared to wild-type, crystals of mutant K52M are very fragile and show only a limited diffraction quality
TGT in complex with 6-amino-4-{2-[(cyclohexylmethyl)amino]ethyl}-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one, residues Val45 and Leu68 form a hydrophobic surface that hosts the cyclohexane ring
wild-type at pH 5.5 to 1.9 A resolution and in complex with pre-queuine 0 to 1.7 A resolution (both crystals belong to space group C2), and in complex with its natural substrate pre-queuine 1 to 2.4 A resolution (crystal belongs to space group C2221). Mutant Y106F alone to 1.95 A resolution and in complex with pre-queuine 1 to 1.9 A resolution (both crystals belong to space group C2). By macroseeding and the hanging-drop method