Large conformational changes in the catalytic cycle of glutathione synthase.
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.[1]References
- Large conformational changes in the catalytic cycle of glutathione synthase. Gogos, A., Shapiro, L. Structure (Camb.) (2002) [Pubmed]
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