7XEN
SufS with L-penicillamine
Summary for 7XEN
| Entry DOI | 10.2210/pdb7xen/pdb |
| Descriptor | Cysteine desulfurase SufS, (2~{R})-3-methyl-2-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-sulfanyl-butanoic acid (3 entities in total) |
| Functional Keywords | cysteine desulfurase, inhibitor, biosynthetic protein |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 |
| Total number of polymer chains | 1 |
| Total formula weight | 46964.92 |
| Authors | Nakamura, R.,Fujishiro, T. (deposition date: 2022-03-31, release date: 2023-04-05, Last modification date: 2025-04-02) |
| 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 (2.47 Å) |
Structure validation
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