4OOT
X-ray structure of the protein-gold adduct formed upon reaction of Aubipic with hen egg white lysozyme
Summary for 4OOT
| Entry DOI | 10.2210/pdb4oot/pdb |
| Related | 4OOO |
| Descriptor | Lysozyme C, GOLD ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Gallus gallus (bantam,chickens) |
| Total number of polymer chains | 1 |
| Total formula weight | 15086.30 |
| Authors | Merlino, A. (deposition date: 2014-02-04, release date: 2014-12-17, Last modification date: 2024-11-27) |
| Primary citation | Messori, L.,Cinellu, M.A.,Merlino, A. Protein Recognition of Gold-Based Drugs: 3D Structure of the Complex Formed When Lysozyme Reacts with Aubipy(c.). ACS Med Chem Lett, 5:1110-1113, 2014 Cited by PubMed Abstract: The structure of the adduct formed in the reaction between Aubipy(c), a cytotoxic organogold(III) compound, and the model protein hen egg white lysozyme (HEWL) has been solved by X-ray crystallography. It emerges that Aubipy(c), after interaction with HEWL, undergoes reduction of the gold(III) center followed by detaching of the cyclometalated ligand; the resulting naked gold(I) ion is found bound to the protein at Gln121. A direct comparison between the present structure and those previously solved for the lysozyme adducts with other gold(III) compounds demonstrates that coordinated ligands play a key role in the protein-metallodrug recognition process. Structural data support the view that gold(III)-based antitumor prodrugs are activated through metal reduction. PubMed: 25313321DOI: 10.1021/ml500231b PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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