8AJ5
X-ray structure of lysozyme obtained upon reaction with [VIVO(malt)2] (Structure B)
This is a non-PDB format compatible entry.
Summary for 8AJ5
| Entry DOI | 10.2210/pdb8aj5/pdb |
| Descriptor | Lysozyme, SODIUM ION, VANADATE ION, ... (8 entities in total) |
| Functional Keywords | metallodrug, vanadium, oxidovanadium, covalent binding, non-covalent binding, protein-metal interaction, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 15464.99 |
| Authors | Paolillo, M.,Merlino, A.,Ferraro, G. (deposition date: 2022-07-27, release date: 2022-11-23, Last modification date: 2024-11-06) |
| Primary citation | Ferraro, G.,Paolillo, M.,Sciortino, G.,Garribba, E.,Merlino, A. Multiple and Variable Binding of Pharmacologically Active Bis(maltolato)oxidovanadium(IV) to Lysozyme. Inorg.Chem., 61:16458-16467, 2022 Cited by PubMed Abstract: The interaction with proteins of metal-based drugs plays a crucial role in their transport, mechanism, and activity. For an active ML complex, where L is the organic carrier, various binding modes (covalent and non-covalent, single or multiple) may occur and several metal moieties (M, ML, ML, etc.) may interact with proteins. In this study, we have evaluated the interaction of [VO(malt)] (bis(maltolato)oxidovanadium(IV) or BMOV, where malt = maltolato, i.e., the common name for 3-hydroxy-2-methyl-4-pyran-4-onato) with the model protein hen egg white lysozyme (HEWL) by electrospray ionization mass spectrometry, electron paramagnetic resonance, and X-ray crystallography. The multiple binding of different V-containing isomers and enantiomers to different sites of HEWL is observed. The data indicate both non-covalent binding of -[VO(malt)(HO)] and [VO(malt)(HO)] and covalent binding of [VO(HO)] and -[VO(malt)] and other V-containing fragments to the side chains of Glu35, Asp48, Asn65, Asp87, and Asp119 and to the C-terminal carboxylate. Our results suggest that the multiple and variable interactions of potential VOL drugs with proteins can help to better understand their solution chemistry and contribute to define the molecular basis of the mechanism of action of these intriguing molecules. PubMed: 36205235DOI: 10.1021/acs.inorgchem.2c02690 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.31 Å) |
Structure validation
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