Analysis of the stability of mutant lysozymes at position 15 using X-ray crystallography

Journal of Biochemistry

Volumn 122, Issue 3, 1997, Pages 512-517

  Ohmura, Tadahiro ^a   Ueda, Tadashi ^a   Motoshima, Hiroyuki ^a   Tamura, Tomohiro ^a   Imoto, Taiji ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

Hen lysozyme; Hydrogen bond; Hydrophobicity; Protein stability; X ray crystallography

Indexed keywords

ALANINE; GLYCINE; HISTIDINE; LYSOZYME; MUTANT PROTEIN; PHENYLALANINE; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME STABILITY; HEN; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

EID: 0030760233     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021782     Document Type: Article

References (23)

1. Matsumura, M., Becktel, W.J., and Matthews, B.W. (1988) Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature 334, 406-410
2. Yutani, K., Ogasahara, K., Tsujita, T., and Sugino, Y. (1987) Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α-subunit. Proc. Natl. Acad. Sci. USA 84, 4441-4444
3. Sandberg, W.S. and Terwilliger, T.C. (1989) Influence of interior packing and hydrophobicity on the stability of a protein. Science 245, 54-57
4. Karpusas, M., Baase, W.A., Matsumura, M., and Matthews, B.W. (1989) Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. Proc. Natl. Acad. Sci. USA 86, 8237-8241
5. Malcolm, B.A., Wilson, K.P., Matthews, B.W., Kirsch, J.F., and Wilson, A.C. (1990) Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing. Nature 345, 86-89
6. Jackson, S.E., Moracci, M., elMasry, N., Johnson, C.M., and Fersht, A.R. (1993) Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32, 11259-11269
7. Buckle, A.M., Henrick, K., and Fersht, A.R. (1993) Crystal structural analysis of mutations in the hydrophobic cores of barnase. J. Mol. Biol. 234, 847-860
8. Kraulis, P.J. (1991) MOLSCRIPT. A program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24, 946-950
9. Blake, C.C.F., Koenig, D.F., Mair, G.A., North, A.C.T., Phillips, D.C., and Sarma, V.R. (1965) Structure of hen egg white lysozyme, a three dimensional Fourier synthesis at 2 A resolution. Nature 206, 757-761
10. Shih, P. and Kirsch, J.F. (1995) Design and structural analysis of an engineered thermostable chicken lysozyme. Protein Sci. 4, 2063-2072
11. Hashimoto, Y., Yamada, K., Motoshima, H., Omura, T., Yamada, H., Yasukochi, T., Miki, T., Ueda, T., and Imoto, T. (1996) A mutation study of catalytic residue Asp 52 in hen egg lysozyme. J. Biochem. 119, 145-150
12. Ueda, T., Tamura, T., Maeda, Y., Hashimoto, Y., Miki, T., Yamada, H., and Imoto, T. (1993) Stabilization of lysozyme by the introduction of Gly-Pro sequence. Protein Eng. 6, 183-187
13. Pace, N.C. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280
14. a of glutamic acid-35. Biochemistry 31, 5545-5553
15. Brunger, A.T. (1992) X-PLOR Manual Ver. 3.1, Yale University, NH, USA
16. Nozaki, Y. and Tanford, C. (1971) The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. J. Biol. Chem. 246, 2211-2217
17. Imoto, T., Ueda, T., Tamura, T., Isakari, Y., Abe, Y., Inoue, M., Miki, T., Kawano, K., and Yamada, H. (1994) Lysozyme requires fluctuation of the active site for the manifestation of activity. Protein Eng. 7, 743-748
18. Ito, Y., Yamada, H., Nakamura, M., Yoshikawa, A., Ueda, T., and Imoto, T. (1993) The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme. Eur. J. Biochem. 213, 649-658
19. Halliday, J.A., Bell, K., McKenzie, H.A., and Shaw, D.C. (1990) Feline whey proteins: identification, isolation and initial characterization of alpha-lactalbumin, beta-lactoglobulin and lysozyme. Comp. Biochem. Physiol. 95B, 773-779
20. Jolles, J., Schoentgen, F., Jolles, P., Prager, E.M., and Wilson, A.C. (1976) Amino acid sequence and immunological properties of chalchalaca egg white lysozyme. J. Mol. Evol. 8, 59-78
21. Pakula, A.A. and Sauer, R.T. (1990) Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature 344, 363-364
22. Alber, T., Sun, D.P., Wilson, K., Wozniak, J.A., Cook, S.P., and Matthews, B.W. (1987) Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature 330, 41-46
23. Bondi, A. (1964) van der Waals volumes, radii. J. Phys. Chem. 68, 441-451