Role of the N-terminal extension of the (βα)-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity

Biochemistry

Volumn 44, Issue 50, 2005, Pages 16405-16412

  Schneider, Birgit ^a,b,d   Knöchel, Thorsten ^c,e   Darimont, Beatrice ^c,f   Hennig, Michael ^c,g   Dietrich, Susanne ^a   Babinger, Karin ^a   Kirschner, Kasper ^c   Sterner, Reinhard ^a,b  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b UNIVERSITY OF COLOGNE   (Germany)

^c UNIVERSITY OF BASEL   (Switzerland)

^d GOETHE UNIVERSITY   (Germany)

^e MERCK KGAA   (Germany)

^f UNIVERSITY OF OREGON   (United States)

^g F HOFFMANN LA ROCHE LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CATALYST ACTIVITY; ESCHERICHIA COLI; NITROGEN COMPOUNDS; OLIGOMERS;

INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE (IGPS); MICHAELIS CONSTANTS; PROTEIN STABILITY; PROTEOLYSIS;

ENZYMES;

AMINO ACID; ANTHRANILIC ACID DERIVATIVE; GUANIDINE; INDOLE 3 GLYCEROL PHOSPHATE SYNTHASE; ISOMERASE; PHOSPHATE; TRYPSIN; TRYPTOPHAN; TRYPTOPHAN SYNTHASE;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME STABILITY; ESCHERICHIA COLI; GENE; GENE EXPRESSION; MICHAELIS CONSTANT; NONHUMAN; OLIGOMERIZATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; SULFOLOBUS SOLFATARICUS; THERMOTOGA MARITIMA;

AMINO ACID SEQUENCE; BASE SEQUENCE; BIOPOLYMERS; CATALYSIS; DNA PRIMERS; ENZYME STABILITY; HYDROLYSIS; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SULFOLOBUS SOLFATARICUS; THERMOTOGA MARITIMA;

ESCHERICHIA COLI; SULFOLOBUS SOLFATARICUS; THERMOTOGA MARITIMA;

EID: 29244461447     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051640n     Document Type: Article

References (28)

1. 8-barrel enzymes, Curr. Opin. Chem. Biol. 7, 252-264.
2. Wise, E. L., and Rayment, I. (2004) Understanding the importance of protein structure to nature's routes for divergent evolution in TIM barrel enzymes, Acc. Chem. Res. 37, 149-158.
3. 8-barrel enzyme fold, Chem. Rev. 105, 4038-4055.
4. 8-barrel enzymes, Biol. Chem. 382, 1315-1320.
5. Gerlt, J. A., Babbitt, P. C., and Rayment, I. (2005) Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity, Arch. Biochem. Biophys. 433, 59-70.
6. 8 barrels: implications for the evolution of metabolic pathways. J. Mol. Biol. 303, 627-641.
7. Wilmanns, M., Hyde, C. C., Davies, D. R., Kirschner, K., and Jansonius, J. N. (1991) Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis, Biochemistry 30, 9161-9169.
8. Stehlin, C., Dahm, A., and Kirschner, K. (1997) Deletion mutagenesis as a test of evolutionary relatedness of indoleglycerol phosphate synthase with other TIM barrel enzymes, FEBS Lett. 403, 268-272.
9. Hennig, M., Darimont, B., Sterner, R., Kirschner, K., and Jansonius, J. N. (1995) 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability, Structure 3, 1295-1306.
10. Merz, A., Knöchel, T., Jansonius, J. N., and Kirschner, K. (1999) The Hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges, J. Mol. Biol. 288, 753-763.
11. Beismann-Driemeyer, S., and Sterner, R. (2001) Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex, J. Biol. Chem. 276, 20387-20396.
12. Merz, A., Knöchel, T., Jansonius, J. N., and Kirschner, K. (1999) The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges, J. Mol. Biol. 288, 753-763.
13. 8-barrel enzymes from different metabolic pathways: sequence requirements and molecular analysis, J. Mol. Biol. 337, 871-879.
14. Hommel, U., Eberhard, M., and Kirschner, K. (1995) Phosphoribosyl anthranilate isomerase catalyzes a reversible Amadori reaction, Biochemistry 34, 5429-5439.
15. Eberhard, M., Tsai-Pflugfelder, M., Bolewska, K., Hommel, U., and Kirschner, K. (1995) Indoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains, Biochemistiy 34, 5419-5428.
16. Sterner, R., Kleemann, G. R., Szadkowski, H., Lustig, A., Hennig, M., and Kirschner, K. (1996) Phosphoribosyl anthranilate isomerase from Thermotoga maritime is an extremely stable and active homodimer, Protein Sci. 5, 2000-2008.
17. The CCP4 suite (1994) Programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763.
18. Brünger, A. T. (1992) X-PLOR Version 3.1. A system for X-ray crystallography and NMR, Yale University Press, New Haven, CT.
19. Knöchel, T. R., Hennig, M., Merz, A., Darimont, B., Kirschner, K., and Jansonius, J. N. (1996) The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: effects of ionic strength, J. Mol. Biol. 262, 502-515.
20. Knöchel, T., Pappenberger, A., Jansonius, J. N., and Kirschner, K. (2002) The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges, J. Biol. Chem. 277, 8626-8634.
21. Merz, A., Yee, M. C., Szadkowski, H., Pappenberger, G., Crameri, A., Stemmer, W. P., Yanofsky, C., and Kirschner, K. (2000) Improving the catalytic activity of a thermophilic enzyme at low temperatures, Biochemistry 39, 880-889.
22. Andreotti, G., Cubellis, M. V., Palo, M. D., Fessas, D., Sannia, G., and Marino, G. (1997) Stability of a thermophilic T1M-barrel enzyme: indole-3-glycerol phosphate synthase from the thermophilic archaeon Sulfolobus solfataricus. Biochem. J. 323, 259-264.
23. 8 barrels, J. Mol. Biol. 320, 1119-1133.
24. Hennig, M., Darimont, B. D., Jansonius, J. N., and Kirschner, K. (2002) The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product, J. Mol. Biol. 319, 757-766.
25. Darimont, B., Stehlin, C., Szadkowski, H., and Kirschner, K. (1998) Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli. Protein Sci. 7, 1221-1232.
26. Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
27. Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
28. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.