Structural and functional basis for substrate specificity and catalysis of levan fructotransferase

Journal of Biological Chemistry

Volumn 287, Issue 37, 2012, Pages 31233-31241

  Park, Jinseo ^a   Kim, Myung Il ^a   Park, Young Don ^c   Shin, Inchul ^a   Cha, Jaeho ^c   Kim, Chul Ho ^d   Rhee, Sangkee ^a,b  

^a Seoul National University   (South Korea)

^b Seoul National University   (South Korea)

^c Pusan National University   (South Korea)

^d Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ARTHROBACTER; C-DOMAIN; CARBOHYDRATE RECOGNITION; CATALYTIC MECHANISMS; FUNCTIONAL BASIS; GLYCOSIDE HYDROLASES; LOOP REGIONS; MOLECULAR BASIS; SIDE CHAIN RESIDUES; STRUCTURAL ELEMENTS; SUBSITES; SUBSTRATE SPECIFICITY; TRANSFER REACTION; TWO-DOMAIN STRUCTURES;

BINDING SITES; CARBOHYDRATES; CATALYSIS; ENZYMES; FRUCTOSE; GLUCOSE; QUANTUM CHEMISTRY; SUGAR (SUCROSE);

SUBSTRATES;

FRUCTOSE; LEVAN FRUCTOTRANSFERASE; LEVANBIOSE; SUCROSE; TRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTHROBACTER; ARTHROBACTER UREAFACIENS; ARTICLE; BETA SHEET; BINDING SITE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; RESIDUE ANALYSIS; STRUCTURE ANALYSIS;

ARTHROBACTER; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DISACCHARIDES; HEXOSYLTRANSFERASES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

ARTHROBACTER UREAFACIENS;

EID: 84866117237     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.389270     Document Type: Article

References (33)

1. Vijn, I., and Smeekens, S. (1999) Fructan. More than a reserve carbohydrate? Plant Physiol. 120, 351-360
2. Valluru, R., and Van den Ende, W. (2008) Plant fructans in stress environments. Emerging concepts and future prospects. J. Exp. Bot. 59, 2905-2916
3. Van den Ende, W., De Coninck, B., and Van Laere, A. (2004) Plant fructan exohydrolases. A role in signaling and defense? Trends Plant Sci. 9, 523-528
4. Meng, G., and Fütterer, K. (2003) Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nat. Struct. Biol. 10, 935-941
5. Strube, C. P., Homann, A., Gamer, M., Jahn, D., Seibel, J., and Heinz, D. W. (2011) Polysaccharide synthesis of the levansucrase SacB from Bacillus megaterium is controlled by distinct surface motifs. J. Biol. Chem. 286, 17593-17600
6. Pijning, T., Anwar, M. A., Böger, M., Dobruchowska, J. M., Leemhuis, H., Kralj, S., Dijkhuizen, L., and Dijkstra, B. W. (2011) Crystal structure of inulosucrase from Lactobacillus. Insights into the substrate specificity and product specificity of GH68 fructansucrases. J. Mol. Biol. 412, 80-93
7. Lammens, W., Le Roy, K., Schroeven, L., Van Laere, A., Rabijns, A., and Van den Ende, W. (2009) Structural insights into glycoside hydrolase family 32 and 68 enzymes. Functional implications. J. Exp. Bot. 60, 727-740
8. Song, K., Bae, K., Lee, Y., Lee, K., and Rhee, S. (2000) Characteristics of levan fructotransferase from Arthrobacter ureafaciens K2032 and difructose anhydride IV formation from levan. Enzyme Microb. Technol. 27, 212-218
9. Cha, J., Park, N. H., Yang, S. J., and Lee, T. H. (2001) Molecular and enzymatic characterization of a levan fructotransferase from Microbacterium sp. AL-210. J. Biotechnol. 91, 49-61
10. Saito, K., and Tomita, F. (2000) Difructose anhydrides. Their mass-production and physiological functions. Biosci. Biotechnol. Biochem. 64, 1321-1327
11. Jung, W. S., Hong, C. K., Lee, S., Kim, C. S., Kim, S. J., Kim, S. I, and Rhee, S. (2007) Structural and functional insights into intramolecular fructosyl transfer by inulin fructotransferase. J. Biol. Chem. 282, 8414-8423
12. Kim, C. H., Jang, E. K., Kim, S. H., Jang, K. H., Kang, S. A., Song, K. B., Kwon, O. S., and Rhee, S. K. (2005) Molecular cloning of levan fructotransferase gene from Arthrobacter ureafaciens K2032 and its expression in Escherichia coli for the production of difructose dianhydride IV. Lett. Appl. Microbiol. 40, 228-234
13. Ritsema, T., and Smeekens, S. (2003) Fructans. Beneficial for plants and humans. Curr. Opin. Plant Biol. 6, 223-230
14. García-Moreno, M. I., Benito, J. M., Mellet, C. O., and Fernández, J. M. (2008) Chemical and enzymatic approaches to carbohydrate-derived spiroketals. Di-D-fructose dianhydrides (DFAs). Molecules 13, 1640-1670
15. Henrissat, B., and Davies, G. (1997) Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7, 637-644
16. Naumoff, D. G. (2011) Hierarchical classification of glycoside hydrolases. Biochemistry 76, 622-635
17. Rayment, I., Rypniewski, W. R., Schmidt-Bäse, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G., and Holden, H. M. (1993) Three-dimensional structure of myosin subfragment-1. A molecular motor. Science 261, 50-58
18. Walter, T. S., Meier, C., Assenberg, R., Au, K. F., Ren, J., Verma, A., Nettleship, J. E., Owens, R. J., Stuart, D. I., and Grimes, J. M. (2006) Lysine methylation as a routine rescue strategy for protein crystallization. Structure 14, 1617-1622
19. Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 267, 307-326
20. Terwilliger, T. C., and Berendzen, J. (1999) Automated MAD and MIR structure solution. Acta Crystallogr. D Biol. Crystallogr. 55, 849-861
21. Terwilliger, T. C. (2000) Maximum-likelihood density modification. Acta Crystallogr. D Biol. Crystallogr. 56, 965-972
22. Emsley, P., Lohkamp, B., Scott, W. G., and Cowtan, K. (2010) Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486-501
23. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Crystallography & NMR system. A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921
24. Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., McCoy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) PHENIX. A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221
25. Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G., McCoy, A., McNicholas, S. J., Murshudov, G. N., Pannu, N. S., Potterton, E. A., Powell, H. R., Read, R. J., Vagin, A., and Wilson, K. S. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242
26. Moon, K. O., Choi, K. H., Kang, H. Y., Oh, J. I., Jang, S. B., Park, C. S., Lee, J. H., and Cha, J. (2008) Probing the critical residues for intramolecular fructosyl transfer reaction of a levan fructotransferase. J. Microbiol. Biotechnol. 18, 1064-1069
27. Song, E. K., Kim, H., Sung, H. K., and Cha, J. (2002) Cloning and characterization of a levanbiohydrolase from Microbacterium laevaniformans ATCC 15953. Gene 291, 45-55
28. Davies, G. J., Wilson, K. S., and Henrissat, B. (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321, 557-559
29. Liu, J., and Waterhouse, A. L. (1992) Conformational analysis of levanbiose by molecular mechanics. Carbohydr. Res. 232, 1-15
30. Nagem, R. A., Rojas, A. L., Golubev, A. M., Korneeva, O. S., Eneyskaya, E. V., Kulminskaya, A. A., Neustroev, K. N., and Polikarpov, I. (2004) Crystal structure of exo-inulinase from Aspergillus awamori. The enzyme fold and structural determinants of substrate recognition. J. Mol. Biol. 344, 471-480
31. Holm, L., and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138
32. Álvaro-Benito, M., Sainz-Polo, M. A., González- Pérez, D., González, B., Plou, F. J., Fernández-Lobato, M., and Sanz-Aparicio, J. (2012) Structural and kinetic insights reveal that the amino acid pair Gln-228/Asn-254 modulates the transfructosylating specificity of Schwanniomyces occidentalis β-fructofuranosidase, an enzyme that produces prebiotics. J. Biol. Chem. 287, 19674-19686
33. Schubot, F. D., Kataeva, I. A., Chang, J., Shah, A. K., Ljungdahl, L. G., Rose, J. P., and Wang, B. (2004) Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum. Biochemistry 43, 1163-1170