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1m0w
From Proteopedia
Yeast Glutathione Synthase Bound to gamma-glutamyl-cysteine, AMP-PNP and 2 Magnesium Ions
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
1M0W is a Single protein structure of sequence from Saccharomyces cerevisiae. 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 Sat May 3 00:29:51 2008
Categories: Glutathione synthase | Saccharomyces cerevisiae | Single protein | Burley, S K. | Gogos, A. | NYSGXRC, New York Structural GenomiX Research Consortium. | Shapiro, L. | Amine/carboxylate ligase | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomic
