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Preliminary X‐ray crystallographic analysis of glutathione transferase zeta 1 (GSTZ1a‐1a)
Author(s) -
Boone Christopher D.,
Zhong Guo,
Smeltz Marci,
James Margaret O.,
McKenna Robert
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x13033591
Subject(s) - transferase , dimer , chemistry , glutathione , crystallography , tyrosine , cytosol , x ray , resolution (logic) , enzyme , stereochemistry , biochemistry , physics , organic chemistry , artificial intelligence , computer science , quantum mechanics
Glutathione transferase zeta 1 (GSTZ1‐1) is a homodimeric enzyme found in the cytosol and mitochondrial matrix of the liver and other tissues. It catalyzes the glutathione‐dependent isomerization of maleylacetoacetate to fumarylacetoacetate in the tyrosine catabolic pathway and can metabolize small halogenated carboxylic acids. GSTZ1a‐1a crystals diffracted to a resolution of 3.1 Å and belonged to space group P 1, with unit‐cell parameters a = 42.0, b = 49.6, c = 54.6 Å, α = 82.9, β = 69.9, γ = 73.4°, with a calculated Matthews coefficient of 2.1 Å 3 Da −1 assuming a dimer in the crystallographic asymmetric unit. Refinement of the structure is currently in progress.