1M0W
Yeast Glutathione Synthase Bound to gamma-glutamyl-cysteine, AMP-PNP and 2 Magnesium Ions
Summary for 1M0W
| Entry DOI | 10.2210/pdb1m0w/pdb |
| Related | 1M0T 2HGS |
| Descriptor | glutathione synthetase, MAGNESIUM ION, SULFATE ION, ... (6 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 | 114040.48 |
| 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 Cited by 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: 12467574DOI: 10.1016/S0969-2126(02)00906-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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