Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B

Biochemical Journal

Volumn 382, Issue 3, 2004, Pages 967-973

  Jang, Do Soo ^a   Cha, Hyung Jin ^a   Cha, Sun Shin ^a   Hong, Bee Hak ^a   Hat, Nam Chul ^a,b   Lee, Ja Young ^a   Oh, Byung Ha ^a   Lee, Heung Soo ^a   Choi, Kwan Yong ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

^b Pusan National University   (South Korea)

Author keywords

Coupling energy; Double mutant cycle; Hydrogen bond network; Ketosteroid isomerase; Site directed mutagenesis

Indexed keywords

AMINO ACIDS; CATALYSIS; CRYSTAL STRUCTURE; DIFFUSION; ENZYMES; ISOMERIZATION;

DOUBLE-MUTANT CYCLE ANALYSIS; HYDROGEN BOND NETWORKS;

HYDROGEN BONDS;

MUTANT PROTEIN; STEROID DELTA ISOMERASE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENERGY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME ISOLATION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; ISOMERIZATION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; PSEUDOMONAS PUTIDA;

BINDING SITES; CATALYSIS; CRYSTALLIZATION; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN DENATURATION; PSEUDOMONAS PUTIDA; RECOMBINANT PROTEINS; STEROID ISOMERASES; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 4744361169     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031871     Document Type: Article

References (35)

1. Carter, P. (1985) Site-directed mutagenesis. Biochem. J. 237, 1-7
2. Botstein, D. and Shortle, D. (1985) Strategies and applications of in vitro mutagenesis. Science 229, 1193-1201
3. Horovitz, A. (1996) Double-mutant cycles: a powerful tool for analyzing protein structure and function. Fold Des. 1, R121-R126
4. Wells, J. A. (1990) Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517
5. Fersht, A. R., Matouschek, A. and Serrano, L. (1992) The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-782
6. Serrano, L., Horovitz, A., Avron, B., Bycroft, M. and Fersht, A. R. (1990) Estimating the contribution of engineered surface electrostatic interaction to protein stability by using double-mutant cycles. Biochemistry 29, 9343-9352
7. Mildvan, A. S., Weber, D. J. and Kuliopulos, A. (1992) Quantitative interpretations of double mutations of enzyme. Arch. Biochem. Biophys. 294, 327-340
8. Vaughan, C. K., Harryson, P., Buckle, A. M. and Fersht, A. R. (2002) A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase. Acta Crystallogr. D. Biol. Crystallogr. 58, 591-600
9. 5-steroid isomerase. Arch. Biochem. Biophys. 370, 9-15
10. 5-3-ketosteroid isomerase. Curr. Opin. Struct. Biol. 11, 674-678
11. 5-3-ketosteroid isomerase from Pseudomonas testosteroni. Gene 58, 257-264
12. 5-3-ketosteroid isomerase of Pseudomonas testosteroni. Gene 69, 121-129
13. 5-3-ketosteroid isomerase of Pseudomonas testosteroni: overexpression of the protein. Proc. Natl. Acad. Soc. U.S.A. 94, 8893-8897
14. 5-3-ketosteroid isomerase with and without a reaction intermediate. Biochemistry 36, 14030-14036
15. 5-steroid isomerase. Science 276, 415-418
16. 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate. Biochemistry 37, 14701-14712
17. 5-3-ketosteroid isomerase from Pseudomonas testosteroni. Biochemistry 37, 8325-8330
18. Kuliopulos, A., Mildvan, A. S. and Talalay, P. (1990) Combined effect of two mutations of catalytic residues on the ketosteroid isomerase reaction. Biochemistry 29, 10271-10280
19. 5-3-ketosteroid isomerase from Pseudomonas putida biotype B. J. Bacteriol. 176, 6672-6676
20. Kim, D. H., Jang, D. S., Nam, G. H., Choi, G., Kim, J. S., Ha, N. C., Kim, M. S., Oh, B.-H. and Choi, K. Y. (2000) Contribution of the hydrogen-bond network involving a tyrosine triad in the active site to the structure and function of a highly proficient ketosteroid isomerase from Pseudomonas putida biotype B. Biochemistry 39, 4581-4589
21. Otwinowski, Z. (1993) in Proceedings of the CCP4 Study Weekend (Sawyer, L., Isaacs, N. and Bailey, S., eds.), pp. 56-62, SERC Daresbury Laboratory, Warrington
22. Brunger, A. T. (1992) X-PLOR, version 3.0, Yale University Press, New Haven
23. Richards, F. M. (1977) Area, volumes, packing, and protein structure. Annu. Rev. Biophys. Bioeng. 6, 151-176
24. Nam, G. H., Jang, D. S., Cha, S. S., Lee, T. H., Kim, D. H., Hong, B. H., Yun, Y. S., Oh, B.-H. and Choi, K. Y. (2001) Maintenance of α-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B. Biochemistry 40, 13529-13537
25. Faiman, G. A. and Horovitz, A. (1996) On the choice of reference mutant states in the application of the double-mutant cycle method. Protein Eng. 9, 315-316
26. Plapp, B. V. (1995) Site-directed mutagenesis: a tool for studying enzyme catalysis. Methods Enzymol. 249, 91-119
27. Fersht, A. R. (1999) Protein engineering in structure and mechanism. Protein Science: a Guide to Enzyme Catalysis and Protein Folding, pp. 420-456, Freeman, New York
28. 2 engineering: structural and functional roles of highly conserved active site residues tyrosine-52 and tyrosine-73. Biochemistry 31, 6402-6413
29. 2: increased hydrophobic interactions of the phenyl groups compensate for the disrupted hydrogen bonds of the tyrosines. Protein Sci. 1, 1585-1594
30. 5-3-ketosteroid isomerase from Pseudomonas putida biotype B. Biochemistry 40, 6828-6835
31. 5-3-ketosteroid isomerase from Pseudomonas testosteroni. Biochemistry 40, 3967-3973
32. 5-3-ketosteroid isomerase. Biochemistry 35, 1525-1532
33. 5-3-ketosteroid isomerase in complexes with diamagnetic and paramagnetic steroids. Biochemistry 36, 3458-3472
34. Chen, Y. W., Fersht, A. R. and Henrick, K. (1993) Contribution of buried hydrogen bonds to protein stability: the crystal structures of two barnase mutants. J. Mol. Biol. 234, 1158-1170
35. 2 from functional perspective. 1. Functionally relevant solution structure and roles of the hydrogen-bonding network. Biochemistry 38, 2908-2918