2ab6
HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE
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OverviewOverview
Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in, Escherichia coli and purified by GSH-affinity chromatography. The, recombinant enzyme and the protein isolated from human tissue were, indistinguishable based on physicochemical, enzymatic and immunological, criteria. The catalytically active dimeric hGSTM2-2 was crystallized, without GSH or other active-site ligands in two crystal forms. Diffraction, from form A crystals extends to 2.5 A and is consistent with the space, group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two, monomers in the asymmetric unit. Diffraction from form B crystals extends, to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c, = 225.9 A) with two dimers in the asymmetric unit. This is the first, report of ligand-free mu-class GST crystals, and a comparison with, liganded complexes will provide insight into the structural consequences, of substrate binding which are thought to be important for catalysis.
About this StructureAbout this Structure
2AB6 is a Single protein structure of sequence from Homo sapiens with GSM as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
ReferenceReference
Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2., Patskovska LN, Fedorov AA, Patskovsky YV, Almo SC, Listowsky I, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):458-60. PMID:9761928
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