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From Proteopedia
Polyoxidovanadate interaction with proteins: crystal structure of lysozyme bound to tetra-vanadate ion (structure 1)
Structural highlights
FunctionLYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1] Publication Abstract from PubMedHigh-resolution crystal structures of lysozyme in the presence of the potential drug V(IV) O(acetylacetonato)(2) under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of V(IV) to V(V) and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V(4) O(12) ](4-) , which interacts with lysozyme non-covalently, and the unprecedented [V(20) O(54) (NO(3) )](n-) , which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules. Stabilization and Binding of [V(4) O(12) ](4-) and Unprecedented [V(20) O(54) (NO(3) )](n-) to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug V(IV) O(acetylacetonato)(2).,Ferraro G, Tito G, Sciortino G, Garribba E, Merlino A Angew Chem Int Ed Engl. 2023 Dec 11;62(50):e202310655. doi: , 10.1002/anie.202310655. Epub 2023 Oct 13. PMID:37768728[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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