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Literature summary for 1.13.11.20 extracted from
- The 3-His metal coordination site promotes the coupling of oxygen activation to cysteine oxidation in cysteine dioxygenase (2020), Biochemistry, 59, 2022-2031 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structures of C93E and cross-linked and non-cross-linked wild-type CDO, to 1.91, 2.49, and 2.30 A, respectively. Mutant C93E has similar overall structural properties compared to cross-linked CDO, but the iron is coordinated by a 3-His/1-Glu geometry. The hydroxyl group of Tyr157 shifts in both non-cross-linked and C93E CDO, and this displacement prevents the residue from participating in substrate stabilization | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C93E | mutation to the corresponding residue of cupin to reestablish the common 3-His/1-Glu metal ligand of the cupin superfamily. Mutant shows dioxygen consumption, which, is not coupled with L-cysteine oxidation. Substrate analogues (D-cysteine, cysteamine, and 3-mercaptopropionate) show variable coordinations to the iron center, but are not viable substrates for the variant | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | P21816 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CDO1 | - |
Rattus norvegicus |
| cysteine dioxygenase type 1 | - |
Rattus norvegicus |
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Release 2023.1 (January 2023)
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