1M0T

Yeast Glutathione Synthase

Summary for 1M0T

• Entry DOI: 10.2210/pdb1m0t/pdb
• Related: 1M0W 2HGS
• Descriptor: glutathione synthetase, SULFATE ION (3 entities in total)
• Functional Keywords: amine/carboxylate ligase, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, ligase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 112334.26

Authors

Gogos, A.,Shapiro, L.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2002-06-14, release date: 2002-12-11, Last modification date: 2024-02-14)

Primary citation

Gogos, A.,Shapiro, L.
Large Conformational Changes in the Catalytic Cycle of Glutathione Synthase
Structure, 10:1669-1676, 2002

PubMed Abstract: 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.

PubMed: 12467574
DOI: 10.1016/S0969-2126(02)00906-1

Experimental method

X-RAY DIFFRACTION (2.3 Å)