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A new crystal structure for the adduct formed in the reaction between AuSac2, a cytotoxic homoleptic gold(I) compound with the saccharinate ligand, and the model protein hen egg white lysozymeA new crystal structure for the adduct formed in the reaction between AuSac2, a cytotoxic homoleptic gold(I) compound with the saccharinate ligand, and the model protein hen egg white lysozyme
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 PubMedA new crystal structure is reported here for the adduct formed in the reaction between NH4 [Au(Sac)2], AuSac2, a cytotoxic homoleptic gold(I) complex with the saccharinate ligand, and the model protein hen egg white lysozyme. To produce this adduct, AuSac2 breaks down and releases both saccharinate ligands. The resulting Au(I) ions bind the protein to ND1 and NE2 atoms of His15 but also to SD atom of the zero-solvent accessible Met105 side chain, which is located in the protein hydrophobic box. The unexpected existence of this secondary gold(I) binding site is confirmed by spectroscopic and spectrometric measurements in solution. Structural evidences for a secondary gold binding site in the hydrophobic box of lysozyme.,Ferraro G, Massai L, Messori L, Cinellu MA, Merlino A Biometals. 2015 Jun 9. PMID:26054833[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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