7q0u | pdb_00007q0u
Lysozyme soaked with V(IV)OSO4 and bipy
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 PubMedVanadium compounds have frequently been proposed as therapeutics, but their application has been hampered by the lack of information on the different V-containing species that may form and how these interact with blood and cell proteins, and with enzymes. Herein, we report several resolved crystal structures of lysozyme with bound V(IV) O(2+) and V(IV) OL(2+) , where L=2,2'-bipyridine or 1,10-phenanthroline (phen), and of trypsin with V(IV) O(picolinato)2 and V(V) O2 (phen)(+) moieties. Computational studies complete the refinement and shed light on the relevant role of hydrophobic interactions, hydrogen bonds, and microsolvation in stabilizating the structure. Noteworthy is that the trypsin-V(V) O2 (phen) and trypsin-V(IV) O(OH)(phen) adducts correspond to similar energies, thus suggesting a possible interconversion under physiological/biological conditions. The obtained data support the relevance of hydrolysis of V(IV) and V(V) complexes in the several types of binding established with proteins and the formation of different adducts that might contribute to their pharmacological action, and significantly widen our knowledge of vanadium-protein interactions. Binding of V(IV) O(2+) , V(IV) OL, V(IV) OL2 and V(V) O2 L Moieties to Proteins: X-ray/Theoretical Characterization and Biological Implications.,Santos MFA, Sciortino G, Correia I, Fernandes ACP, Santos-Silva T, Pisanu F, Garribba E, Costa Pessoa J Chemistry. 2022 Apr 29:e202200105. doi: 10.1002/chem.202200105. PMID:35486702[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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