Literature summary for 3.1.1.29 extracted from

Fromant, M.; Schmitt, E.; Mechulam, Y.; Lazennec, C.; Plateau, P.; Blanquet, S.
Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase (2005), Biochemistry, 44, 4294-4301.

Cloned(Commentary)

Cloned (Comment)	Organism
pth2 gene, expression in Escherichia coli	Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging drop vapour diffusion method, 24°C, 0.0027 ml of 1.3 mg/ml protein in 20 mM Tris-HCl, pH 7.0, 0.1 mM EDTA, and 10 mM 2-mercaptoethanol are mixed with 0.0007 ml of 11 mg/ml tRNAfMet solution and 0.002 ml of reservoir solution containing 0.8 M LiSO4 and 1.6% PEG 8000, crystallization of tRNA free crystals within a few days, X-ray diffraction structure determination and analysis of native and HgBr2-containing crystals at 1.8-3.0 A resolution, modeling	Saccharolobus solfataricus

Crystallization (Comment)

Organism

purified recombinant enzyme, hanging drop vapour diffusion method, 24°C, 0.0027 ml of 1.3 mg/ml protein in 20 mM Tris-HCl, pH 7.0, 0.1 mM EDTA, and 10 mM 2-mercaptoethanol are mixed with 0.0007 ml of 11 mg/ml tRNAfMet solution and 0.002 ml of reservoir solution containing 0.8 M LiSO4 and 1.6% PEG 8000, crystallization of tRNA free crystals within a few days, X-ray diffraction structure determination and analysis of native and HgBr2-containing crystals at 1.8-3.0 A resolution, modeling

Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	Q980V1	gene pth2	-

Reaction

Reaction	Comment	Organism	Reaction ID
N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA	residues K18, D86, and T90 are essential for catalytic activity, they are located in the N-part of alpha1 and in the beta3-beta4 loop. K18 and D86, which form a salt bridge, might play a role in the catalysis thanks to their acid and basic functions, whereas the OH group of T90 could act as a nucleophile	Saccharolobus solfataricus	a

Subunits

Subunits	Comment	Organism
dimer	crystal structure analysis, three-dimensional structure, each protomer is made of a mixed five-stranded beta-sheet surrounded by two groups of two alpha-helices, the dimer interface is mainly formed by van der Waals interactions between hydrophobic residues belonging to the two N-terminal R1 helices contributed by two protomers, overview	Saccharolobus solfataricus

Synonyms

Synonyms	Comment	Organism
peptidyl-tRNA hydrolase	-	Saccharolobus solfataricus
suPth2	-	Saccharolobus solfataricus