7YB3
SufS with D-cysteine for 1 min
Summary for 7YB3
| Entry DOI | 10.2210/pdb7yb3/pdb |
| Descriptor | Cysteine desulfurase SufS, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | cysteine desulfurase, iron-sulfur cluster biosynthesis, plp-dependent enzyme, biosynthetic protein |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 |
| Total number of polymer chains | 1 |
| Total formula weight | 47660.68 |
| Authors | Nakamura, R.,Fujishiro, T. (deposition date: 2022-06-28, release date: 2023-07-05, Last modification date: 2025-04-09) |
| Primary citation | Nakamura, R.,Fujishiro, T. Visualizing thiazolidine ring formation in the reaction of D-cysteine and pyridoxal-5'-phosphate within L-cysteine desulfurase SufS. Biochem.Biophys.Res.Commun., 754:151497-151497, 2025 Cited by PubMed Abstract: The reactivity of pyridoxal-5'-phosphate (PLP) with cysteine and its derivatives has been of increasing interest because the corresponding product, a thiazolidine PLP-cysteine adduct, can be formed via PLP-dependent enzymatic and non-enzymatic reactions. Here, we report biochemical and X-ray crystallographic snapshots of thiazolidine formation in reaction of D-cysteine with PLP in SufS, a PLP-dependent L-cysteine desulfurase. By comparing L- and D-penicillamine-bound SufS showing no thiazolidine formation in the crystals with D-cysteine SufS, we proposed a thiazolidine formation mechanism with important factors: the polar environments provided by the carbonyl groups of Ala28-Ala29 and Lys224-mediated base catalysis for the nucleophilic thiolate of D-cysteine. PubMed: 40020322DOI: 10.1016/j.bbrc.2025.151497 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
