1OAS
O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM
Summary for 1OAS
| Entry DOI | 10.2210/pdb1oas/pdb |
| Descriptor | O-ACETYLSERINE SULFHYDRYLASE, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | cystein biosynthesis, beta replacement enzyme, plp dependent enzyme, homodimer, lyase |
| Biological source | Salmonella typhimurium |
| Total number of polymer chains | 2 |
| Total formula weight | 69435.13 |
| Authors | Burkhard, P.,Rao, G.S.J.,Hohenester, E.,Schnackerz, K.D.,Cook, P.F.,Jansonius, J.N. (deposition date: 1999-01-29, release date: 2000-01-28, Last modification date: 2023-12-27) |
| Primary citation | Burkhard, P.,Rao, G.S.,Hohenester, E.,Schnackerz, K.D.,Cook, P.F.,Jansonius, J.N. Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. J.Mol.Biol., 283:121-133, 1998 Cited by PubMed Abstract: The last step in cysteine biosynthesis in enteric bacteria is catalyzed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase. Here we report the crystal structure at 2.2 A resolution of the A-isozyme of O-acetylserine sulfhydrylase isolated from Salmonella typhimurium. O-acetylserine sulfhydrylase shares the same fold with tryptophan synthase-beta from Salmonella typhimurium but the sequence identity level is below 20%. There are some major structural differences: the loops providing the interface to the alpha-subunit in tryptophan synthase-beta and two surface helices of tryptophan synthase-beta are missing in O-acetylserine sulfhydrylase. The hydrophobic channel for indole transport from the alpha to the beta active site of tryptophan synthase-beta is, not unexpectedly, also absent in O-acetylserine sulfhydrylase. The dimer interface, on the other hand, is more or less conserved in the two enzymes. The active site cleft of O-acetylserine sulfhydrylase is wider and therefore more exposed to the solvent. A possible binding site for the substrate O-acetylserine is discussed. PubMed: 9761678DOI: 10.1006/jmbi.1998.2037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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