8OM8
X-ray structure of lysozyme obtained upon reaction with [VIVO(empp)2] (Structure A)
This is a non-PDB format compatible entry.
Summary for 8OM8
| Entry DOI | 10.2210/pdb8om8/pdb |
| Descriptor | Lysozyme C, ACETATE ION, tris-[(1-methyl-2-ethyl-3-hydroxy-4(1H)-pyridinone)]-V(V)3O7, ... (7 entities in total) |
| Functional Keywords | metallodrugs, protein metalation, biologically active v compounds, metal-protein interactions, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 15543.45 |
| Authors | Paolillo, M.,Ferraro, G.,Merlino, A. (deposition date: 2023-03-31, release date: 2023-06-07, Last modification date: 2024-11-13) |
| Primary citation | Ferraro, G.,Paolillo, M.,Sciortino, G.,Pisanu, F.,Garribba, E.,Merlino, A. Implications of Protein Interaction in the Speciation of Potential V IV O-Pyridinone Drugs. Inorg.Chem., 62:8407-8417, 2023 Cited by PubMed Abstract: Vanadium complexes (VCs) are promising agents for the treatment, among others, of diabetes and cancer. The development of vanadium-based drugs is mainly limited by a scarce knowledge of the active species in the target organs, which is often determined by the interaction of VCs with biological macromolecules like proteins. Here, we have studied the binding of [VO(empp)] (where Hempp is 1-methyl-2-ethyl-3-hydroxy-4(1)-pyridinone), an antidiabetic and anticancer VC, with the model protein hen egg white lysozyme (HEWL) by electrospray ionization-mass spectrometry (ESI-MS), electron paramagnetic resonance (EPR), and X-ray crystallography. ESI-MS and EPR techniques reveal that, in aqueous solution, both the species [VO(empp)] and [VO(empp)(HO)], derived from the first one upon the loss of a empp(-) ligand, interact with HEWL. Crystallographic data, collected under different experimental conditions, show covalent binding of [VO(empp)(HO)] to the side chain of Asp48, and noncovalent binding of -[VO(empp)(HO)], [VO(empp)(HO)], [VO(empp)(HO)], and of an unusual trinuclear oxidovanadium(V) complex, [VO(empp)(HO)], with accessible sites on the protein surface. The possibility of covalent and noncovalent binding with different strength and of interaction with various sites favor the formation of adducts with the multiple binding of vanadium moieties, allowing the transport in blood and cellular fluids of more than one metal-containing species with a possible amplification of the biological effects. PubMed: 37195003DOI: 10.1021/acs.inorgchem.3c01041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.08 Å) |
Structure validation
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