1Y7L
O-Acetylserine Sulfhydrylase Complex
Summary for 1Y7L
| Entry DOI | 10.2210/pdb1y7l/pdb |
| Descriptor | O-acetylserine sulfhydrylase, decamer fragment of Serine acetyltransferase, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | x-ray crystallography; sulfhydrylase, transferase |
| Biological source | Haemophilus influenzae More |
| Cellular location | Cytoplasm (By similarity): P43886 |
| Total number of polymer chains | 2 |
| Total formula weight | 34808.70 |
| Authors | Huang, B.,Vetting, M.W.,Roderick, S.L. (deposition date: 2004-12-09, release date: 2005-04-26, Last modification date: 2023-11-15) |
| Primary citation | Huang, B.,Vetting, M.W.,Roderick, S.L. The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. J.Bacteriol., 187:3201-3205, 2005 Cited by PubMed Abstract: The biosynthesis of cysteine in bacteria and plants is carried out by a two-step pathway, catalyzed by serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS; O-acetylserine [thiol] lyase). The aerobic form of OASS forms a tight bienzyme complex with SAT in vivo, termed cysteine synthase. We have determined the crystal structure of OASS in complex with a C-terminal peptide of SAT required for bienzyme complex formation. The binding site of the peptide is at the active site of OASS, and its C-terminal carboxyl group occupies the same anion binding pocket as the alpha-carboxylate of the O-acetylserine substrate of OASS. These results explain the partial inhibition of OASS by SAT on complex formation as well as the competitive dissociation of the complex by O-acetylserine. PubMed: 15838047DOI: 10.1128/JB.187.9.3201-3205.2005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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