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T4 lysozyme (T4 L) is a protein-ligand complex specific to gram-negative bacteriophages of the T4 family. The three-dimensional structure of T4 L was determined at high resolution by X-ray crystallography. The T4 L structure consists of two sub-domains with a parallel beta-sheet structure in the central region. The ligand binding is at the interface between the two sub-domains. The three ligands, ethyl beta-D-1-thio-galactopyranoside (TGN), neoglycolipid II and monomaleate 4-beta-D-Galp 1-OMe, inhibit the crystallization of the protein. Two models of the TGN-binding site on T4 L are suggested by NMR spin relaxation methods. The X-ray crystallographic structures of TGN-T4 L and neoglycolipid II-T4 L complexes are also determined, revealing the neoglycolipid II binding to the interfacial region.Specific physical activities as predictors of physical activity in adolescents: an observational study.
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