The 1.5 Å structure of endo-1,3-β-glucanase from Streptomyces sioyaensis: Evolution of the active-site structure for 1,3-β-glucan-binding specificity and hydrolysis

Acta Crystallographica Section D: Biological Crystallography

Volumn 64, Issue 9, 2008, Pages 964-970

  Hong, Tang Yao ^a   Hsiao, Yu Yuan ^b,c   Meng, Menghsiao ^b   Li, TienHsiung Thomas ^b  

^a TAJEN UNIVERSITY   (Taiwan)

^b NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^c INSTITUTE OF MOLECULAR BIOLOGY   (Taiwan)

Author keywords

Endo 1,3 glucanases; Glycosyl hydrolases

Indexed keywords

NOCARDIOPSIS SP.; STREPTOMYCES; STREPTOMYCES SIOYAENSIS;

BETA 1,3 GLUCAN; BETA GLUCAN; BETA-1,3-GLUCAN; GLUCAN ENDO 1,3 BETA GLUCOSIDASE;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYMOLOGY; METABOLISM; STREPTOMYCES; X RAY CRYSTALLOGRAPHY;

BETA-GLUCANS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GLUCAN ENDO-1,3-BETA-D-GLUCOSIDASE; MODELS, MOLECULAR; STREPTOMYCES;

EID: 49749127692     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444908021550     Document Type: Article

References (30)

1. Chen, C. H., Huang, J. W. & Tzeng, D. S. (2000). Plant Pathol. Bull. 9, 193.
2. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
3. Cruz, J. de la, Pintor-Toro, J. A., Benitez, T., Llobell, A. & Romero, L. C. (1995). J. Bacteriol. 177, 6937-6945.
4. Fibriansah, G., Masuda, S., Koizumi, N., Nakamura, S. & Kumasaka, T. (2007). Proteins, 69, 683-690.
5. Frishman, D. & Argos, P. (1995). Proteins, 23, 566-579.
6. Gaiser, O. J., Piotukh, K., Ponnuswamy, M. N., Planas, A., Borriss, R. & Heinemann, U. (2006). J. Mol. Biol. 357, 1211-1225.
7. Grenier, J., Potvin, C. & Asselin, A. (1993). Plant Physiol. 103, 1277-1283.
8. Gueguen, Y., Voorhorst, W. G., van der Oost, J. & de Vos, W. M. (1997). J. Biol. Chem. 272, 31258-31264.
9. Hahn, M., Olsen, O., Politz, O., Borriss, R. & Heinemann, U. (1995). J. Biol. Chem. 270, 3081-3088.
10. Hahn, M., Pons, J., Planas, A., Querol, E. & Heinemann, U. (1995). FEBS Lett. 374, 221-224.
11. Henrissat, B. (1991). Biochem. J. 208, 309-316.
12. Hong, T. Y., Cheng, C. W., Huang, J. W. & Meng, M. H. (2002). Microbiology, 148, 1151-1159.
13. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
14. Juncosa, M., Pons, J., Dot, T., Querol, E. & Planas, A. (1994). J. Biol. Chem. 269, 14530-14535.
15. Lamzin, V. S., Perrakis, A. & Wilson, K. S. (2001). International Tables for Crystallography, Vol. F, edited by M. G. Rossmann & E. Arnold, pp. 720-722. Dordrecht: Kluwer Academic Publishers.
16. Masuda, S., Endo, K., Koizumi, N., Hayami, T., Fukazawa, T., Yatsunami, R., Fukui, T. & Nakamura, S. (2006). Extremophiles, 10, 251-255.
17. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Acta Cryst. D53, 240-255.
18. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
19. Perrakis, A., Sixma, T. K., Wilson, K. S. & Lamzin, V. S. (1997). Acta Cryst. D53, 448-455.
20. Petřek, M., Otyepka, M., Banáš, P., Košinová, P., Koča, J. & Damborský, J. (2006). BMC Bioinformatics, 7, 316.
21. Potterton, L., McNicholas, S., Krissinel, E., Gruber, J., Cowtan, K., Emsley, P., Murshudov, G. N., Cohen, S., Perrakis, A. & Noble, M. (2004). Acta Cryst. D60, 2288-2294.
22. Receveur-Brechot, V., Czjzek, M., Barre, A., Roussel, A., Peumans, W. J., Van Damme, E. J. M. & Rouge, P. (2006). Proteins, 63, 235-242.
23. Selitrennikoff, C. P. (2001). Appl. Environ. Microbiol. 67, 2883-2894.
24. Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.
25. Tempel, W., Liu, Z.-J., Horanyi, P. S., Deng, L., Lee, D., Newton, M. G., Rose, J. P., Ashida, H., Li, S. C., Li, Y. T. & Wang, B.-C. (2005). Proteins, 59, 141-144.
26. Tsai, L. C., Shyur, L. F., Lee, S. H., Lin, S. S. & Yuan, H. S. (2003). J. Mol. Biol. 330, 607-620.
27. Varghese, J. N., Garrett, T. P., Colman, P. M., Chen, L., Hoj, P. B. & Fincher, G. B. (1994). Proc. Natl Acad. Sci. USA, 91, 2785-2789.
28. Watanabe, T., Kasahara, N., Aida, K. & Tanaka, H. (1992). J. Bacteriol. 174, 186-190.
29. Wood, T. M. & Bhat, K. M. (1988). Methods Enzymol. 160, 87-112.
30. Yi, S. Y. & Hwang, B. K. (1997). Mol. Cell, 7, 408-413.