Literature summary for 2.5.1.18 extracted from

Grahn, E.; Novotny, M.; Jakobsson, E.; Gustafsson, A.; Grehn, L.; Olin, B.; Madsen, D.; Wahlberg, M.; Mannervik, B.; Kleywegt, G.J.
New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix (2006), Acta crystallogr. Sect. D, 62, 197-207.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified isozyme GST A1-1 in complex with substrate glutathione, hanging drop vapour diffusion method, room temperature, 10 mg/ml protein in 0.1 M Tris-HCl, pH 8.5, with 19% methyl PEG 2000, 0.03 M sodium acetate, pH 4.6, and 1% 2-mercaptoethanol for the apoenzyme, or in 0.1 M TrisHCl, pH 7.8, with 24% PEG 4000, and 1% 2-mercaptoethanol, with glutathione for wild-type and mutant enzyme complexed with the substrate, the mutant apoenzyme is crystallized from 0.1 M TrisHCl, pH 7.8, with 24% PEG 4000, 2 mM DTT and 30% MPD, X-ray diffraction structure determination and analysis at 2.0 A resolution	Homo sapiens

Crystallization (Comment)

Organism

purified isozyme GST A1-1 in complex with substrate glutathione, hanging drop vapour diffusion method, room temperature, 10 mg/ml protein in 0.1 M Tris-HCl, pH 8.5, with 19% methyl PEG 2000, 0.03 M sodium acetate, pH 4.6, and 1% 2-mercaptoethanol for the apoenzyme, or in 0.1 M TrisHCl, pH 7.8, with 24% PEG 4000, and 1% 2-mercaptoethanol, with glutathione for wild-type and mutant enzyme complexed with the substrate, the mutant apoenzyme is crystallized from 0.1 M TrisHCl, pH 7.8, with 24% PEG 4000, 2 mM DTT and 30% MPD, X-ray diffraction structure determination and analysis at 2.0 A resolution

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
T68E	site-directed mutagenesis, crystal structure comparison with the wild-type isozyme GST-A1-1, overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	alpha class GST A1-1	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes from Escherichia coli by cation exchange chromatography and S-hexylglutathione affinity chromatography, respectively	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	glutathione binds in the G site of the isozyme GST-A1-1, glutathione binding alone is sufficient to stabilize the C-terminal helix of the protein	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
dimer	homodimer, C-terminal region structure of isozyme GST-A1-1, which can adopt an ordered helix-like structure even in the apo state, but shows a strong tendency to unwind, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
glutathione transferase A1-1	-	Homo sapiens