7N2T
O-acetylserine sulfhydrylase from Citrullus vulgaris in the internal aldimine state, with citrate bound
Summary for 7N2T
| Entry DOI | 10.2210/pdb7n2t/pdb |
| Descriptor | Cysteine synthase, CITRIC ACID, PENTAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | o-acetylserine sulfhydrylase, plp, cysteine synthase, biosynthetic protein |
| Biological source | Citrullus lanatus subsp. vulgaris (watermelon) |
| Total number of polymer chains | 1 |
| Total formula weight | 36204.26 |
| Authors | Smith, J.L.,Buller, A.R.,Bingman, C.A. (deposition date: 2021-05-29, release date: 2022-07-06, Last modification date: 2024-04-03) |
| Primary citation | Smith, J.L.,Harrison, I.M.,Bingman, C.A.,Buller, A.R. Investigation of beta-Substitution Activity of O-Acetylserine Sulfhydrolase from Citrullus vulgaris. Chembiochem, 23:e202200157-e202200157, 2022 Cited by PubMed Abstract: Pyridoxal-5'-phosphate (PLP)-dependent enzymes have garnered interest for their ability to synthesize non-standard amino acids (nsAAs). One such class of enzymes, O-acetylserine sulfhydrylases (OASSs), catalyzes the final step in the biosynthesis of l-cysteine. Here, we examine the β-substitution capability of the OASS from Citrullus vulgaris (CvOASS), a putative l-mimosine synthase. While the previously reported mimosine synthase activity was not reproducible in our hands, we successfully identified non-native reactivity with a variety of O-nucleophiles. Optimization of reaction conditions for carboxylate and phenolate substrates led to distinct conditions that were leveraged for the preparative-scale synthesis of nsAAs. We further show this enzyme is capable of C-C bond formation through a β-alkylation reaction with an activated nitroalkane. To facilitate understanding of this enzyme, we determined the crystal structure of the enzyme bound to PLP as the internal aldimine at 1.55 Å, revealing key features of the active site and providing information that may guide subsequent development of CvOASS as a practical biocatalyst. PubMed: 35476889DOI: 10.1002/cbic.202200157 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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