8RTJ

X-ray structure of lysozyme obtained upon reaction with [VIVO(8-HQ)2] in ethylene glycol

This is a non-PDB format compatible entry.

Summary for 8RTJ

• Entry DOI: 10.2210/pdb8rtj/pdb
• Descriptor: Lysozyme C, SODIUM ION, 2,2-bis($l^{1}-oxidanyl)-3-oxa-1$l^{4}-aza-2$l^{4}-vanadatricyclo[6.3.1.0^{4,12}]dodeca-1(12),4,6,8,10-pentaene, ... (6 entities in total)
• Functional Keywords: vanadium compound, lysozyme, protein metalation, hydrolase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 15192.24

Authors

Paolillo, M.,Ferraro, G.,Merlino, A. (deposition date: 2024-01-26, release date: 2025-02-12, Last modification date: 2025-07-16)

Primary citation

Paolillo, M.,Ferraro, G.,Pisanu, F.,Marechal, J.D.,Sciortino, G.,Garribba, E.,Merlino, A.
Protein-Protein Stabilization in V IV O/8-Hydroxyquinoline-Lysozyme Adducts.
Chemistry, 30:e202401712-e202401712, 2024

PubMed Abstract: The binding of the potential drug [VO(8-HQ)], where 8-HQ is 8-hydroxyquinolinato, with hen egg white lysozyme (HEWL) was evaluated through spectroscopic (electron paramagnetic resonance, EPR, and UV-visible), spectrometric (electrospray ionization-mass spectrometry, ESI-MS), crystallographic (X-ray diffraction, XRD), and computational (DFT and docking) studies. ESI-MS indicates the interaction of [VO(8-HQ)(HO)] and [VO(8-HQ)(HO)] species with HEWL. Room temperature EPR spectra suggest both covalent and non-covalent binding of the two different V-containing fragments. XRD analyses confirm these findings, showing that [VO(8-HQ)(HO)] interacts covalently with the solvent exposed Asp119, while cis-[VO(8-HQ)(HO)] non-covalently with Arg128 and Lys96 from a symmetry mate. The covalent binding of [VO(8-HQ)(HO)] to Asp119 is favored by a π-π contact with Trp62 and a H-bond with Asn103 of a symmetry-related molecule. Additionally, the covalent binding of VO to Asp48 and non-covalent binding of other V-containing fragments to Arg5, Cys6, and Glu7 are revealed. Molecular docking indicates that, in the absence of the interactions occurring at the protein-protein interface close to Asp119, the covalent binding to Glu35 or Asp52 should be preferred. Such a protein-protein stabilization could be more common than what believed up today, at least in the solid state, and should be considered in the characterization of metal-protein adducts.

PubMed: 38923243
DOI: 10.1002/chem.202401712

Experimental method

X-RAY DIFFRACTION (1.27 Å)