2ab6
HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONEHUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE
Structural highlights
Function[GSTM2_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||