Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity

Acta Crystallographica Section D: Biological Crystallography

Volumn 69, Issue 2, 2013, Pages 298-307

  Lipski, Alexandra ^a   Watzlawick, Hildegard ^b   Ravaud, Stéphanie ^a   Robert, Xavier ^a   Rhimi, Moez ^a   Haser, Richard ^a   Mattes, Ralf ^b   Aghajari, Nushin ^a  

^a INSTITUT DE BIOLOGIE ET CHIMIE DES PROTÉINES   (France)

^b UNIVERSITY OF STUTTGART   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

1 DEOXYNOJIRIMYCIN; BACTERIAL PROTEIN; DISACCHARIDE; DRUG DERIVATIVE; GLUCOSE; GLUCOSYLTRANSFERASE; ISOMALTOSE; LIGAND; PALATINOSE; SUCROSE; SUCROSE ISOMERASE; TREHALULOSE;

ARTICLE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; HYDROLYSIS; METHODOLOGY; MUTATION; RANDOMIZATION; RHIZOBIUM; RHIZOBIUM SP.; X RAY CRYSTALLOGRAPHY;

ISOMALTULOSE; RHIZOBIUM SP.; SUCROSE ISOMERASE; TREHALULOSE;

1-DEOXYNOJIRIMYCIN; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DISACCHARIDES; GLUCOSE; GLUCOSYLTRANSFERASES; HYDROLYSIS; ISOMALTOSE; LIGANDS; MUTATION; RANDOM ALLOCATION; RHIZOBIUM; SUCROSE;

EID: 84873573535     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444912045532     Document Type: Article

References (55)

1. Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K. & Terwilliger, T. C. (2002). Acta Cryst. D58, 1948-1954.
2. Aghajari, N., Feller, G. & Gerday, C. (1998). Protein Sci. 7, 7564-7572.
3. Aroonnual, A., Nihira, T. & Seki, T. (2007). Enzyme Microb. Technol. 40, 1221-1227.
4. Battye, T. G. G., Kontogiannis, L., Johnson, O., Powell, H. R. & Leslie, A. G. W. (2011). Acta Cryst. D67, 271-281.
5. Boel, E., Brady, L., Brzozowski, A. M., Derewenda, Z., Dodson, G. G., Jensen, V. J., Petersen, S. B., Swift, H., Thim, L. & Woldike, H. F. (1990). Biochemistry, 29, 6244-6249.
6. Bru? nger, 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. &Warren, G. L. (1998). Acta Cryst. D54, 905-921.
7. Cantarel, B. L., Coutinho, P. M., Rancurel, C., Bernard, T., Lombard, V. & Henrissat, B. (2009). Nucleic Acids Res. 37, D233-D238.
8. Champion, E., Remaud-Simeon, M., Skov, L. K., Kastrup, J. S., Gajhede, M. & Mirza, O. (2009). Acta Cryst. D65, 1309-1314.
9. Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Cryst. D66, 12-21.
10. Cho, M.-H., Park, S.-E., Lim, J. K., Kim, J.-S., Kim, J. H., Kwon, D. Y. & Park, C.-S. (2007). Biotechnol. Lett. 29, 453-458.
11. Davies, G. & Henrissat, B. (1995). Structure, 3, 853-859.
12. DeLano, W. L. (2002). PyMOL. http://www.pymol.org.
13. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
14. Evans, P. R. (2011). Acta Cryst. D67, 282-292.
15. Go? rl, J., Timm, M. & Seibel, J. (2012). Chembiochem, 13, 149- 156.
16. Goulter, K. C., Hashimi, S. M. & Birch, R. G. (2012). Enzyme Microb. Technol. 50, 57-64.
17. Hayward, S. & Berendsen, H. J. (1998). Proteins, 30, 144-154.
18. Hjerrild, M., Stensballe, A., Jensen, O. N., Gammeltoft, S. & Rasmussen, T. E. (2004). FEBS Lett. 568, 55-59.
19. Holm, L. & Park, J. (2000). Bioinformatics, 16, 566-567.
20. Kabsch, W. (2010). Acta Cryst. D66, 125-132.
21. Kim, M.-I., Kim, H.-S., Jung, J. & Rhee, S. (2008). J. Mol. Biol. 380, 636-647.
22. Koshland, D. E. & Clarke, E. (1953). J. Biol. Chem. 205, 917-924.
23. Krissinel, E. & Henrick, K. (2004). Acta Cryst. D60, 2256-2268.
24. Krissinel, E. & Henrick, K. (2007). J. Mol. Biol. 372, 774-797.
25. Laskowski, R. A. (2001). Nucleic Acids Res. 29, 221-222.
26. Lipski, A., Rhimi, M., Haser, R. & Aghajari, N. (2010). J. Appl. Glycosci. 57, 219-228.
27. MacGregor, E. A., Janecek, S. & Svensson, B. (2001). Biochim. Biophys. Acta, 1546, 1-20.
28. Mattes, R., Klein, K., Schiweck, H., Kunz, M. & Munir, M. (1998). US Patent 5786140.
29. McCoy, A. J. (2007). Acta Cryst. D63, 32-41.
30. Miyata, Y., Sugitani, T., Tsuyuki, K., Ebashi, T. & Nakajima, Y. (1992). Biosci. Biotechnol. Biochem. 56, 1680-1681.
31. Moriarty, N.W., Grosse-Kunstleve, R.W. & Adams, P. D. (2009). Acta Cryst. D65, 1074-1080.
32. Mosi, R., He, S., Uitdehaag, J., Dijkstra, B.W. &Withers, S. G. (1997). Biochemistry, 36, 9927-9934.
33. Murshudov, G. N., Skubá k, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
34. Nagai, Y., Sugitani, T. & Tsuyuki, K. (1994). Biosci. Biotechnol. Biochem. 58, 1789-1793.
35. Navaza, J. (2001). Acta Cryst. D57, 1367-1372.
36. Oslancová, A. & Janecek, S. (2002). Cell. Mol. Life Sci. 59, 1945-1959.
37. Petrey, D. & Honig, B. (2003). Methods Enzymol. 374, 492-509.
38. Ravaud, S., Robert, X., Watzlawick, H., Haser, R., Mattes, R. & Aghajari, N. (2007). J. Biol. Chem. 282, 28126-28136.
39. Ravaud, S., Robert, X., Watzlawick, H., Haser, R., Mattes, R. & Aghajari, N. (2009). FEBS Lett. 583, 1964-1968.
40. Ravaud, S., Robert, X., Watzlawick, H., Laurent, S., Haser, R., Mattes, R. & Aghajari, N. (2008). Biocatal. Biotransformation, 26, 111-119.
41. Ravaud, S., Watzlawick, H., Haser, R., Mattes, R. & Aghajari, N. (2005). Acta Cryst. F61, 100-103.
42. Ravaud, S., Watzlawick, H., Mattes, R., Haser, R. & Aghajari, N. (2005). Biologia, 60, 89-95.
43. Robert, X., Haser, R.,Mori, H., Svensson, B. & Aghajari, N. (2005). J. Biol. Chem. 280, 32968-32978.
44. Roussel, A., Fontecilla-Camps, J. C. & Cambillau, C. (1990). J. Mol. Graph. 8, 86-91.
45. Skov, L. K., Mirza, O., Henriksen, A., De Montalk, G. P., Remaud- Simeon, M., Sarçabal, P., Willemot, R. M., Monsan, P. & Gajhede, M. (2001). J. Biol. Chem. 276, 25273-25278.
46. Tsuyuki, K., Sugitani, T., Miyata, Y., Ebashi, T., Yakajima, T. & Miyata, T. (1984). Caries Res. 18, 47-51.
47. Uitdehaag, J. C., Mosi, R., Kalk, K. H., van der Veen, B. A., Dijkhuizen, L., Withers, S. G. & Dijkstra, B. W. (1999). Nature Struct. Biol. 6, 432-436.
48. Vandermarliere, E., Bourgois, T. M., Winn, M. D., van Campenhout, S., Volckaert, G., Delcour, J. A., Strelkov, S. V., Rabijns, A. & Courtin, C. M. (2009). Biochem. J. 418, 39-47.
49. Veronese, T. & Perlot, P. (1998). FEBS Lett. 441, 348-352.
50. Vester-Christensen, M. B., Abou Hachem, M., Svensson, B. & Henriksen, A. (2010). J. Mol. Biol. 403, 739-750.
51. Watzlawick, H. & Mattes, R. (2009). Appl. Environ. Microbiol. 75, 7026-7036.
52. Weidenhagen, R.(1957). Chem. Ber. 90, 1046-1050.
53. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
54. Wu, L. & Birch, R. G. (2004). J. Appl. Microbiol. 97, 93-103.
55. Zhang, D., Li, N., Lok, S.-M., Zhang, L.-H. & Swaminathan, K. (2003). J. Biol. Chem. 278, 35428-35434.