Lysozyme complexes

Radian, E.A., et al. 5tructure of an antibody-antigen complex. Crystal structure of the HyHEL-10 Fab-lysozyme complex. Proc. Natl. Acad. Sci. USA 86 5938-5942,... 

In this exercise you will examine the interactions between the enzyme lysozyme (Chapter 4) and the Fab portion of the anti-lysozyme antibody. Use the PDB identifier 1FDL to explore the structure of the IgGl Fab fragment-lysozyme complex (antibody-antigen complex). View the structure using Protein Explorer, and also use the information in the PDBsum summary of the structure to answer the following questions. 

Figure 12.5. Summary page of PDBsum. The summary page for human lysozyme complex (1LZC) shows hyperlinks to various structure analyses.

These values are too short to be influenced significantly by Tr, the rotational correlation time of the enzyme-Gd3+ complex, or Tm, the mean residence time of water molecules in the first coordination sphere of the metal. Moreover, the minima in the plots of Tj p vs. Wj2 indicate that Tc must be dominated by Ts, the electron spin relaxation time. The Ts values for Gd + in this system are longer than most of those determined previously for Gd3+. The electron spin relaxation time for aqueous Gd3+ is (4-7) x 10 10s at 30 MHz (42), while values for Ts of (2-7) x 10 10s have been reported for complexes of Gd3+ with pyruvate kinase (37) and a value of 2.2 x 10- s has been found for a Gd 1"-lysozyme complex (36). Moreover, we have estimated a Tc of 6,8 x 10 10s for Gd + bound to parvalbumin.3 The long Gd3+ correlation times found in the present study are consistent with a poor accessibility of these Gd3+ sites to solvent water molecules. 

Tello, and R. J. Poljak, J. Biol. Chem., 266, 12915 (1991). Crystallographic Refinement of the Three-Dimensional Structure of the FabD 1.3-Lysozyme Complex at 2.5 A Resolution. 

Fig. 29. Enzymatic activity of lysozyme as a function of water content (grams of water per gram of sample), at pH 8, 9, and 10. , O, A, Measurements on powders hydrated by isopiestic equilibration ,, A, solvent added to powder. Powder samples were the 1 1 (GlcNAc)6-lysozyme complex, obtained by lyophilization. The reaction rate (no sec ) was determined by product analysis. From Rupley etcd. (1980).

Using both the X-ray structure of the Fab lysozyme complex (Sheriff et al., 1987, 1988 Amit et al., 1986) and the site-specific mutagenesis of... 

T. O. Fischmann, G.A. Bentley, T.N. Bhat, G. Boulot, R.A. Mariuzza, S.E. Phillips, D. Tello, and R.J. Poljak. 1991. Crystallographic refinement of the three-dimensional structure of the FabDl.3-lysozyme complex at 2.5-A resolution J. Biol. Chem. 266 12915-12920. (PubMedl... 

The first crystal structure of an enzyme, that of lysozyme, was determined by David C. Phillips and coworkers " in 1965. The most striking feature in the three-dimensional structure of lysozyme is a prominent cleft that traverses one face of the molecule. The X-ray structure of lysozyme complexed with a three-residue oligosaccharide showed that this cleft was, indeed, the substrate-binding site. The crystal structure of this complex provided the first three-dimensional model for how enyzmes work. 

Slagle, S., R. E. Kozack and S. Subramaniam. (1994). Role of electrostatics in antibody-antigen association anti-hen egg lysozyme/lysozyme complex (HyHEL-5/HEL). J. Biomol. Struct. Dyn. 12 439-56. 

Yamaguchi K., Hachiya K., Moriyama Y., Takeda K. Electrophoretic light scattering study of sodium dextran sulfate-lysozyme complex. J. Coll. Interf. Sci. 1996 179 249-254. 

Figure 3.8 Impedimetric analysis of an aptamer-lysozyme complex nsing [Fe as a redox label.

Madhusudan and Vijajan, M., Additional binding sites in lysozyme. X-ray analysis of lysozyme complexes with bromophenol red and bromophenol blue. Protein Eng., 5(5), 399, 1992. 

Figure 8.4. SD study of the dye eosin in water by third-order photon echo spectroscopy. The peak shift data of eosin in water (sohd circles) and lysozyme complex in water (open triangles) are shown. The inset shows the lysozyme data (open triangles) with fits (solid line). Adapted with permission from J. Phys. Chem. B, 103 (1999), 7995. Copyright (1999) American Chemical Society.

FIGURE 4 Dependence of Lysozyme complex elasticity modulus on MR concentration at frequency 0.007 and 0.625 rad/s. The drop lines indicate the interval of change corresponding parameters for pure LYS. 

As noted previously, lysozyme complexes with and is partially inactivated by red wine phenolics and bentonite. In red wines, utilization may have an indirect sensory impact on palate structure similar to that of proteinaceous fining agents. In white wines, potential protein instability may result from its utilization. Thus, treated wines should be evaluated and treated with bentonite as appropriate. As of this writing, lysozyme is in the process of approval for winemaking purposes. 

Fig. 7 The structure of a ruthenium CO-RM 3/HEWL protein adduct. (Image taken from ref. 61, CORM-3 Reactivity toward Proteins The Crystal Structure of a Ru(ii) Dicarbonyl-Lysozyme Complex, G. J. L. Bernardes, T. Santos-Silva, A. Mukhopadhyay, J. D. Seixas, C. C. Romao and M. J. Romao, J. Am. Chem. Soc. 2011,133,1192-1195. Copyright 2011, American Chemical Society.

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