9RBV

X-ray structure of lysozyme when is treated with Cs2[V(V)2O4(mal)2]2H2O at 310K

これはPDB形式変換不可エントリーです。

9RBV の概要

• エントリーDOI: 10.2210/pdb9rbv/pdb
• 分子名称: Lysozyme C, CHLORIDE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: vanadium compounds, lysozyme, protein metalation, hydrolase
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14456.54

構造登録者

Paolillo, M.,Ferraro, G.,Merlino, A. (登録日: 2025-05-27, 公開日: 2025-08-13, 最終更新日: 2025-10-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.09 Å)