9RBT

X-ray structure of decavanadate/lysozyme adduct obtained when the protein is treated with Cs2[V(V)2O4(mal)2]2H2O (structure B)

This is a non-PDB format compatible entry.

Summary for 9RBT

• Entry DOI: 10.2210/pdb9rbt/pdb
• Descriptor: Lysozyme C, CHLORIDE ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: vanadium compounds, decavanadate, lysozyme, protein metalation, hydrolase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 15783.07

Authors

Paolillo, M.,Ferraro, G.,Merlino, A. (deposition date: 2025-05-27, release date: 2025-08-13, Last modification date: 2025-10-29)

Primary citation

Paolillo, M.,Ferraro, G.,Gumerova, N.I.,Pisanu, F.,Garribba, E.,Rompel, A.,Merlino, A.
Speciation and structural transformation of a V V -malate complex in the absence and in the presence of a protein: from a dinuclear species to decavanadate.
Inorg Chem Front, 12:6503-6518, 2025

PubMed Abstract: A strategy for the development of new vanadium-based drugs is the preparation of complexes that target proteins and bear molecules involved in the cellular metabolism as ligands, like α-hydroxycarboxylic acids. Based on these premises, this study explores the solution behaviour of the dioxidovanadium(V) complex of malic acid, Cs[V O(mal)]·2HO, and its interaction with the model protein lysozyme (HEWL) at room and at physiological temperature using V nuclear magnetic resonance (NMR), electrospray ionisation-mass spectrometry (ESI-MS) and X-ray crystallography. The results show the coexistence in aqueous solution of various molecular species containing two or ten V centres. In solution these species are formed regardless of the presence of HEWL, while at 37 °C the formation of [V O] (V) is precluded when the protein is present. Crystallographic data reveal that, when protein crystals are incubated with the V compound at room temperature (25 °C) and at pH 4.0, [VO], [V O(mal)], [V O] and [V O] are bound to the protein, while at 37 °C, under the same conditions, only [VO] interacts with HEWL. [V O] can bind the protein both covalently (as [V O] ion) and non-covalently. Whereas the transformation of [V O(mal)] to [V O(mal)] is expected on the basis of thermodynamic considerations, the formation of V and of the V-HEWL adduct is not easily predictable. Docking calculations confirm the experimental results and highlight the role of protein-protein interaction in the stabilization of the revealed adduct. This study demonstrates that vanadium compounds can undergo transformation in solution, giving rise to species that interact with proteins through several binding modes and stabilization mechanisms.

PubMed: 40757088
DOI: 10.1039/d5qi01384d

Experimental method

X-RAY DIFFRACTION (1.18 Å)