Crystal structures of Geobacillus stearothermophilus α-glucuronidase complexed with its substrate and products: Mechanistic implications

Journal of Biological Chemistry

Volumn 279, Issue 4, 2004, Pages 3014-3024

  Golan, Gali ^a   Shallom, Dalia ^b,c   Teplitsky, Anna ^a   Zaide, Galia ^b   Shulami, Smadar ^b   Baasov, Timor ^b   Stojanoff, Vivian ^d   Thompson, Andy ^d   Shoham, Yuval ^b,c   Shoham, Gil ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^b TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^c ITT   (United States)

^d EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BIODEGRADATION; CARBOXYLIC ACIDS; CATALYST ACTIVITY; CELLULOSE; CHEMICAL BONDS; CONFORMATIONS; COORDINATION REACTIONS; CRYSTAL STRUCTURE; ENZYME KINETICS; OLIGOMERS;

HEMICELLULOSE; PROTONATION;

BIOCHEMISTRY;

ALPHA GLUCURONIDASE; BETA GLUCURONIDASE; CARBOXYLIC ACID; GENE PRODUCT; HEMICELLULOSE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATALYSIS; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; GEOBACILLUS STEAROTHERMOPHILUS; GLYCOLYSIS; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN STABILITY;

GEOBACTER; GLYCOSIDE HYDROLASES; HYDROLYSIS; MODELS, MOLECULAR; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

ANIMALIA; BACTERIA (MICROORGANISMS); GEOBACILLUS; GEOBACILLUS STEAROTHERMOPHILUS;

EID: 9144241621     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M310098200     Document Type: Article

References (61)

1. Shoham, Y., Lamed, R., and Bayer, E. A. (1999) Trends Microbiol. 7, 275-281
2. Shallom, D., and Shoham, Y. (2003) Curr. Opin. Microbiol. 6, 219-228
3. Schwarz, W. H. (2001) Appl. Microbiol. Biotechnol. 56, 634-649
4. Bourne, Y., and Henrissat, B. (2001) Curr. Opin. Struct. Biol. 11, 593-600
5. Wolfenden, R., Lu, X., and Young, G. (1998) J. Am. Chem. Soc. 120, 6814-6815
6. Zechel, D. L., and Withers, S. G. (1999) Acc. Chem. Res. 33, 11-18
7. Biely, P., Vrsanska, M., Tenkanen, M., and Kluepfel, D. (1997) J. Biotechnol. 57, 151-166
8. Biely, P., de Vries, R. P., Vrsanska, M., and Visser, J. (2000) Biochim. Biophys. Acta 1474, 360-364
9. Nurizzo, D., Nagy, T., Gilbert, H. J., and Davies, G. J. (2002) Structure 10, 547-556
10. Gilead, S., and Shoham, Y. (1995) Appl. Environ. Microbiol. 61, 170-174
11. Bravman, T., Zolotnitsky, G., Belakhov, V., Shoham, G., Henrissat, B., Baasov, T., and Shoham, Y. (2003) Biochemistry 42, 10528-10536
12. Bravman, T., Mechaly, A., Shulami, S., Belakhov, V., Baasov, T., Shoham, G., and Shoham, Y. (2001) FEBS Lett. 495, 115-119
13. Gat, O., Lapidot, A., Alchanati, I., Regueros, C., and Shoham, Y. (1994) Appl. Environ. Microbiol. 60, 1889-1896
14. Shallom, D., Belakhov, V., Solomon, D., Shoham, G., Baasov, T., and Shoham, Y. (2002) J. Biol. Chem. 277, 43667-43673
15. Shulami, S., Gat, O., Sonenshein, A. L., and Shoham, Y. (1999) J. Bacteriol. 181, 3695-3704
16. Zaide, G., Shallom, D., Shulami, S., Zolotnitsky, G., Golan, G., Baasov, T., Shoham, G., and Shoham, Y. (2001) Eur. J. Biochem. 268, 3006-3016
17. Mechaly, A., Teplitsky, A., Belakhov, V., Baasov, T., Shoham, G., and Shoham, Y. (2000) J. Biotechnol. 78, 83-86
18. Milner, Y., and Avigad, G. (1967) Carbohydr. Res. 4, 359-361
19. Teplitsky, A., Shulami, S., Moryles, S., Zaide, G., Shoham, Y., and Shoham, G. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 869-872
20. Hendrickson, W. A., and Ogata, C. M. (1997) Methods Enzymol. 276, 494-523
21. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 407-426
22. Terwilliger, T. C., and Berendzen, J. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 1872-1877
23. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard. (1991) Acta Crystallogr. Sect. A 47, 110-119
24. Navaza, J. (1994) Acta Cryst. Sect. A 50, 157-163
25. Brunger, 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) Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
26. Brunger, A. T. (1992) Nature 355, 472-475
27. Luzzati, P. V. (1952) Acta Crystallogr. Sect. D 5, 802-805
28. Nagy, T., Nurizzo, D., Davies, G. J., Biely, P., Lakey, J. H., Bolam, D. N., and Gilbert, H. J. (2003) J. Biol. Chem. 278, 20286-20292
29. Holm, L., and Sander, C. (1998) Nucleic Acids Res. 26, 316-319
30. Mark, B. L., Vocadlo, D. J., Knapp, S., Triggs-Raine, B. L., Withers, S. G., and James, M. N. (2001) J. Biol. Chem. 276, 10330-10337
31. Tews, I., Perrakis, A., Oppenheim, A., Dauter, Z., Wilson, K. S., and Vorgias, C. E. (1996) Nat. Struct. Biol. 3, 638-648
32. Davies, G., and Henrissat, B. (1995) Structure 3, 853-859
33. Ly, H. D., and Withers, S. G. (1999) Annu. Rev. Biochem. 68, 487-522
34. Wicki, J., Rose, D. R., and Withers, S. G. (2002) Methods Enzymol. 354, 84-105
35. Bronnenmeier, K., Meissner, H., Stocker, S., and Staudenbauer, W. L. (1995) Microbiology 141, 2033-2040
36. Uchida, H., Nanri, T., Kawabata, Y., Kusakabe, I., and Murakami, K. (1992) Biosci. Biotechnol. Biochem. 56, 1608-1615
37. Tenkanen, M., and Siika-aho, M. (2000) J. Biotechnol. 78, 149-161
38. Wood, T. M., and Wilson, C. A. (1995) Appl. Microbiol. Biotechnol. 43, 893-900
39. Davies, G., Sinnott, M. L., and Withers, S. G. (1998) in Comprehensive Biological Catalysis (Sinnott, M. L., ed) Vol. 1, pp. 119-209, Academic Press Ltd., London
40. Sinnott, M. L. (1990) Chem. Rev. 90, 1171-1202
41. Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R., and Huber, R. (1997) J. Mol. Biol. 267, 865-880
42. van Santen, Y., Benen, J. A., Schroter, K. H., Kalk, K. H., Armand, S., Visser, J., and Dijkstra, B. W. (1999) J. Biol. Chem. 274, 30474-30480
43. Armand, S., Wagemaker, M. J., Sanchez-Torres, P., Kester, H. C., van Santen, Y., Dijkstra, B. W., Visser, J., and Benen, J. A. (2000) J. Biol. Chem. 275, 691-696
44. Shimizu, T., Nakatsu, T., Miyairi, K., Okuno, T., and Kato, H. (2002) Biochemistry 41, 6651-6659
45. Joshi, M. D., Sidhu, G., Nielsen, J. E., Brayer, G. D., Withers, S. G., and McIntosh, L. P. (2001) Biochemistry 40, 10115-10139
46. Ramasubbu, N., Ragunath, C., and Mishra, P. J. (2003) J. Mol. Biol. 325, 1061-1076
47. Varrot, A., Schulein, M., and Davies, G. J. (1999) Biochemistry 38, 8884-8891
48. Dominguez, R., Souchon, H., Lascombe, M., and Alzari, P. M. (1996) J. Mol. Biol. 257, 1042-1051
49. Koivula, A., Ruohonen, L., Wohlfahrt, G., Reinikainen, T., Teeri, T. T., Piens, K., Claeyssens, M., Weber, M., Vasella, A., Becker, D., Sinnott, M. L., Zou, J. Y., Kleywegt, G. J., Szardenings, M., Stahlberg, J., and Jones, T. A. (2002) J. Am. Chem. Soc. 124, 10015-10024
50. Alzari, P. M., Souchon, H., and Dominguez, R. (1996) Structure 4, 265-275
51. McIntosh, L. P., Hand, G., Johnson, P. E., Joshi, M. D., Korner, M., Plesniak, L. A., Ziser, L., Wakarchuk, W. W., and Withers, S. G. (1996) Biochemistry 36, 9958-9966
52. Dall'Acqua, W., and Carter, P. (2000) Protein Sci. 9, 1-9
53. Davies, G. J., Ducros, V. M., Varrot, A., and Zechel, D. L. (2003) Biochem. Soc. Trans. 31, 523-527
54. Vasella, A., Davies, G. J., and Bohm, M. (2002) Curr. Opin. Chem. Biol. 6, 619-629
55. Varrot, A., Macdonald, J., Stick, R. V., Pell, G., Gilbert, H. J., and Davies, G. J. (2003) Chem. Commun. (Camb) 8, 946-947
56. Guerin, D. M., Lascombe, M. B., Costabel, M., Souchon, H., Lamzin, V., Beguin, P., and Alzari, P. M. (2002) J. Mol. Biol. 316, 1061-1069
57. Sabini, E., Sulzenbacher, G., Dauter, M., Dauter, Z., Jorgensen, P. L., Schulein, M., Dupont, C., Davies, G. J., and Wilson, K. S. (1999) Chem. Biol. 6, 483-492
58. Sidhu, G., Withers, S. G., Nguyen, N. T., McIntosh, L. P., Ziser, L., and Brayer, G. D. (1999) Biochemistry 38, 5346-5354
59. McCarter, J. D., and Withers, S. G. (1994) Curr. Opin. Struct. Biol. 4, 885-892
60. Fierobe, H. P., Mirgorodskaya, E., McGuire, K. A., Roepstorff, P., Svensson, B., and Clarke, A. J. (1998) Biochemistry 37, 3743-3752
61. Pickersgill, R., Smith, D., Worboys, K., and Jenkins, J. (1998) J. Biol. Chem. 273, 24660-24664