Crystal structure of Thermotoga maritima α-glucosidase AglA defines a new clan of NAD+-dependent glycosidases

Journal of Biological Chemistry

Volumn 278, Issue 21, 2003, Pages 19151-19158

  Lodge, Jacinta A ^a   Maier, Timm ^a   Liebl, Wolfgang ^b   Hoffmann, Volker ^b   Sträter, Norbert ^a,c  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

^c UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER CONCENTRATION; CRYSTAL STRUCTURE; HYDROLYSIS; MALTOSE; OXIDATION; POSITIVE IONS;

DIVALENT METAL CATIONS;

ENZYMES;

ALPHA GLUCOSIDASE AG1A; BACTERIAL ENZYME; GLYCOSIDASE; MALTOSE; MANGANESE; NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; ALPHA GLUCOSIDASE; BACTERIAL PROTEIN;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME ISOLATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; THERMOTOGA MARITIMA; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; CRYSTALLIZATION; DIMERIZATION; ENZYMOLOGY; HYDROGEN BOND; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; THERMOTOGA MARITIMA;

ALPHA-GLUCOSIDASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HYDROGEN BONDING; MALTOSE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; NAD; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; THERMOTOGA MARITIMA;

EID: 0038820035     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M211626200     Document Type: Article

References (44)

1. Wolfenden, R., Lu, X., and Young, G. (1998) J. Am. Chem. Soc. 120, 6814-6815
2. Zechel, D. L., and Withers, S. G. (2000) Acc. Chem. Res. 33, 11-18
3. Rye, C. S., and Withers, S. G. (2000) Curr. Opin. Chem. Biol. 4, 573-580
4. Koshland, D. E. (1953) Biol. Rev. Camb. Philos. Soc. 28, 416-436
5. Raasch, C., Streit, W., Schanzer, J., Bibel, M., Gosslar, U., and Liebl, W. (2000) Extremophiles 4, 189-200
6. Thompson, J., Pikis, A., Ruvinov, S. B., Henrissat, B., Yamamoto, H., and Sekiguchi, J. (1998) J. Biol. Chem. 273, 27347-27356
7. Thompson, J., Gentry-Weeks, C. R., Nguyen, N. Y., Folk, J. E., and Robrish, S. A. (1995) J. Bacteriol. 177, 2505-2512
8. Robrish, S. A., Fales, H. M., Gentry-Weeks, C., and Thompson, J. (1994) J. Bacteriol. 176, 3250-3256
9. Suresh, C., Rus'd, A. A., Kitaoka, M., and Hayashi, K. (2002) FEBS Lett. 517, 159-162
10. Raasch, C., Armbrecht, M., Streit, W., Hocker, B., Strater, N., and Liebl, W. (2002) FEBS Lett. 517, 267-271
11. Thompson, J., Ruvinov, S. B., Freedberg, D. I., and Hall, B. G. (1999) J. Bacteriol. 181, 7339-7345
12. Fierobe, H. P., Clarke, A. J., Tull, D., and Svensson, B. (1998) Biochemistry 37, 3753-3759
13. Liljestrom, P. L., and Liljestrom, P. (1987) Nucleic Acids Res. 15, 2213-2220
14. Thompson, J., Robrish, S. A., Immel, S., Lichtenthaler, F. W., Hall, B. G., and Pikis, A. (2001) J. Biol. Chem. 276, 37415-37425
15. Otwinowski, Z. (1993) in Proceedings of the CCP4 Study Weekend: Data Collection and Processing (Sawyer, L., Isaacs, N., and Bailey, S., eds) pp. 56-62, SERC Daresbury Laboratory, Warrington, United Kingdom
16. Terwilliger, T. C., and Berendzen, J. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 849-861
17. de la Fortelle, E., and Bricogne, G. (1997) Methods Enzymol. 276, 472-494
18. Collaborative Computational Project 4 (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
19. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sect. A 47, 110-119
20. Castagnetto, J. M., Hermessy, S. W., Roberts, V. A., Getzoff, E. D., Tainer, J. A., and Pique, M. E. (2002) Nucleic Acids Res. 30, 379-382
21. Kleywegt, G. J., and Jones, T. A. (1996) Acta Crystallogr. Sect. D Biol. Crystallogr. 52, 826-828
22. Kleywegt, G. J. (1997) J. Mol. Biol. 273, 371-376
23. Kleywegt, G. J. (1996) Acta Crystallogr. Sect. D Biol. Crystallogr. 52, 842-857
24. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, N., 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
25. Svergun, D. I., Barberato, C., and Koch, M. H. J. (1995) J. Appl. Crystallogr. 28, 768-773
26. Corpet, F. (1988) Nucleic Acids Res. 16, 10881-10890
27. Gouet, P., Courcelle, E., Stuart, D. I., and Metoz, F. (1999) Bioinformatics (Oxf.) 15, 305-308
28. Westhead, D. R., Slidel, T. W. F., Flores, T. P. J., and Thornton, J. M. (1999) Protein Sci. 8, 897-904
29. Holm, L., and Sander, C. (1993) J. Mol. Biol. 233, 123-138
30. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
31. Lawrence, M. C., and Bourke, P. (2000) J. Appl. Crystallogr. 33, 990-999
32. Merritt, E. A., and Bacon, D. J. (1997) Methods Enzymol. 277, 505-524
33. Janin, J., and Chothia, C. (1990) J. Biol. Chem. 265, 16027-16030
34. Goodsell, D. S., and Olson, A. J. (2000) Annu. Rev. Biophys. Biomol. Struct. 29, 105-153
35. Orengo, C. A., Michie, A. D., Jones, S., Jones, D. T., Swindells, M. B., and Thornton, J. M. (1997) Structure 5, 1093-1108
36. Chapman, A. D., Cortes, A., Dafforn, T. R., Clarke, A. R., and Brady, R. L. (1999) J. Mol. Biol. 285, 703-712
37. Allard, S. T., Giraud, M. F., Whitfield, C., Graninger, M., Messner, P., and Naismith, J. H. (2001) J. Mol. Biol. 307, 283-295
38. Michel, G., Chantalat, L., Duee, E., Barbeyron, T., Henrissat, B., Kloareg, B., and Dideberg, O. (2001) Structure 9, 513-525
39. Davies, G., and Henrissat, B. (1995) Structure 3, 853-859
40. Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J. K., and Jones, T. A. (1990) Science 249, 380-386
41. Rossman, M. G., Liljas, A., Brandon, C. I., and Banaszak, L. T. (1975) Enzymes 11, 61-102
42. Choi, H. J., Kang, S. W., Yang, C. H., Rhee, S. G., and Ryu, S. E. (1998) Nat. Struct. Biol. 5, 400-406
43. Nagashima, S., Nakasako, M., Dohmae, N., Tsujimura, M., Takio, K., Odaka, M., Yohda, M., Kamiya, N., and Endo, I. (1998)Nat. Struct. Biol. 5, 347-351
44. Fierobe, H. P., Mirgorodskaya, E., McGuire, K. A., Roepstorff, P., Svensson, B., and Clarke, A. J. (1998) Biochemistry 37, 3743-3752