1m0t
From Proteopedia
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Yeast Glutathione Synthase
Overview
Glutathione synthase catalyzes the final ATP-dependent step in glutathione, biosynthesis, the formation of glutathione from gamma-glutamylcysteine and, glycine. We have determined structures of yeast glutathione synthase in, two forms: unbound (2.3 A resolution) and bound to its substrate, gamma-glutamylcysteine, the ATP analog AMP-PNP, and two magnesium ions, (1.8 A resolution). These structures reveal that upon substrate binding, large domain motions convert the enzyme from an open unliganded form to a, closed conformation in which protein domains completely surround the, substrate in the active site.
About this Structure
1M0T is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 as ligand. Active as Glutathione synthase, with EC number 6.3.2.3 Full crystallographic information is available from OCA.
Reference
Large conformational changes in the catalytic cycle of glutathione synthase., Gogos A, Shapiro L, Structure. 2002 Dec;10(12):1669-76. PMID:12467574
Page seeded by OCA on Tue Nov 20 21:02:53 2007
Categories: Glutathione synthase | Saccharomyces cerevisiae | Single protein | Burley, S.K. | Gogos, A. | NYSGXRC, New.York.Structural.GenomiX.Research.Consortium. | Shapiro, L. | SO4 | Amine/carboxylate ligase | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
