6BPS
Crystal structure of cysteine-bound ferrous form of the uncrosslinked F2-Tyr157 human cysteine dioxygenase
Summary for 6BPS
| Entry DOI | 10.2210/pdb6bps/pdb |
| Descriptor | Cysteine dioxygenase type 1, FE (II) ION, CYSTEINE, ... (6 entities in total) |
| Functional Keywords | cysteine, cys-tyr cofactor, iron, unnatural amino acid, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 23815.30 |
| Authors | |
| Primary citation | Li, J.,Griffith, W.P.,Davis, I.,Shin, I.,Wang, J.,Li, F.,Wang, Y.,Wherritt, D.J.,Liu, A. Cleavage of a carbon-fluorine bond by an engineered cysteine dioxygenase. Nat. Chem. Biol., 14:853-860, 2018 Cited by PubMed Abstract: Cysteine dioxygenase (CDO) plays an essential role in sulfur metabolism by regulating homeostatic levels of cysteine. Human CDO contains a post-translationally generated Cys93-Tyr157 cross-linked cofactor. Here, we investigated this Cys-Tyr cross-linking by incorporating unnatural tyrosines in place of Tyr157 via a genetic method. The catalytically active variants were obtained with a thioether bond between Cys93 and the halogen-substituted Tyr157, and we determined the crystal structures of both wild-type and engineered CDO variants in the purely uncross-linked form and with a mature cofactor. Along with mass spectrometry and F NMR, these data indicated that the enzyme could catalyze oxidative C-F or C-Cl bond cleavage, resulting in a substantial conformational change of both Cys93 and Tyr157 during cofactor assembly. These findings provide insights into the mechanism of Cys-Tyr cofactor biogenesis and may aid the development of bioinspired aromatic carbon-halogen bond activation. PubMed: 29942080DOI: 10.1038/s41589-018-0085-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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