Structure of Thermus thermophilus HB8 H-protein of the glycine-cleavage system, resolved by a six-dimensional molecular-replacement method

Acta Crystallographica - Section D Biological Crystallography

Volumn 59, Issue 9, 2003, Pages 1610-1618

  Nakai, Tadashi ^a   Ishijima, Jun ^a   Masui, Ryoji ^a,b   Kuramitsu, Seiki ^a,b   Kamiya, Nobuo ^a  

^a RIKEN Harima Institute/SPring 8 ^*  (Japan)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MULTIENZYME COMPLEX;

ARTICLE; BINDING SITE; CHEMISTRY; METHODOLOGY; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CLONING, MOLECULAR; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; MULTIENZYME COMPLEXES; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); PISUM SATIVUM; THERMUS; THERMUS THERMOPHILUS;

EID: 0041784485     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444903014975     Document Type: Article

References (40)

1. Adachi, S., Oguchi, T., Tanida, H., Park, S. Y., Shimizu, H., Miyatake, H., Kamiya, N., Shiro, Y., Inoue, Y., Ueki, T. & Iizuka, T. (2001). Nucl. Instrum. Methods Phys. Res. A, 467, 711-714.
2. Brünger, A. T. (1990). Acta Cryst. A46, 46-57.
3. Brünger, A. T. (1992). X-PLOR. Version 3.1. A System for X-ray Crystallography and NMR. Yale University, Connecticut, USA.
4. 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. & Warren, G. L. (1998). Acta Cryst. D54, 905-921.
5. Cohen-Addad, C., Faure, M., Neuburger, M., Ober, R., Sieker, L., Bourguignon, J., Macherel, D. & Douce, R. (1997). Biochimie, 79, 637-643.
6. Cohen-Addad, C., Pares, S., Sieker, L., Neuburger, M. & Douce, R. (1995). Nature Struct. Biol. 2, 63-68.
7. Douce, R., Bourguignon, J., Neuburger, M. & Rébeillé F. (2001). Trends Plant Sci. 6, 167-176.
8. Esnouf, R. M. (1997). J. Mol. Graph. 15, 132-134.
9. Faure, M., Bourguignon, J., Neuburger, M., MacHerel, D., Sieker, L., Ober, R., Kahn, R., Cohen-Addad, C. & Douce, R. (2000). Eur. J. Biochem. 267, 2890-2898.
10. Fujiwara, K., Okamura-Ikeda, K. & Motokawa, Y. (1991). FEBS Lett. 293, 115-118.
11. Fujiwara, K., Okamura-Ikeda, K. & Motokawa, Y. (1996). J. Biol. Chem. 271, 12932-12936.
12. Guilhaudis, L., Simorre, J. P., Blackledge, M., Marion, D., Gans, P., Neuburger, M. & Douce, R. (2000). Biochemistry, 39, 4259-4266.
13. Kabsch, W. & Sander, C. (1983). Biopolymers, 22, 2577-2637.
14. Kikuchi, G. & Hiraga, K. (1982). Mol. Cell Biochem. 45, 137-149.
15. Kissinger, C. R., Gehlhaar, D. K. & Fogel, D. B. (1999). Acta Cryst. D55, 484-491.
16. Kissinger, C. R., Gehlhaar, D. K., Smith, B. A. & Bouzida, D. (2001). Acta Cryst. D57, 1474-1479.
17. Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.
18. Laskowski, R. A., Macarthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
19. Li de la Sierra, I., Pernot, L., Prange, T., Saludjian, P., Schiltz, M., Fourme, R. & Padron, G. (1997). J. Mol. Biol. 269, 129-141.
20. Luzzati, V. (1952). Acta Cryst. 5, 802-810.
21. Macherel, D., Bourguignon, J., Forest, E., Faure, M., Cohen-Addad, C. & Douce, R. (1996). Eur. J. Biochem. 236, 27-33.
22. McRee, D. E. (1992). J. Mol. Graph. 10, 44-46.
23. Mande, S. S., Sarfaty, S., Allen, M. D., Perham, R. N. & Hol, W. G. J. (1996). Structure, 4, 277-286.
24. Mattevi, A., Obmolova, G., Kalk, K. H., van Berkel, W. J. & Hol, W. G. (1993). J. Mol. Biol. 230, 1200-1215.
25. Mattevi, A., Obmolova, G., Sokatch, J. R., Betzel, C. & Hol, W. G. (1992). Proteins, 13, 336-351.
26. Mattevi, A., Schierbeck, A. J. & Hol, W. G. (1991). J. Mol. Biol. 220, 975-994.
27. Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.
28. Motokawa, Y., Fujiwara, K. & Okamura-Ikeda, K. (1995). Bithiols in Health and Disease, edited by L. Packer & E. Cadenas, pp. 389-407. New York: Marcel Dekker.
29. Nakai, T., Nakagawa, N., Maoka, N., Masui, R., Kuramitsu, S. & Kamiya, N. (2003). Acta Cryst. D59, 554-557.
30. Navaza, J. (1994). Acta Cryst. A50, 157-163.
31. Neuburger, M., Polidori, A. M., Pietre, E., Faure, M., Jourdain, A., Bourguignon, J., Pucci, B. & Douce, R. (2000). Eur. J. Biochem. 267, 2882-2889.
32. Nicholls, A., Sharp, K. A. & Honig, B. (1991). Proteins Struct. Funct. Genet. 11, 281-296.
33. Okamura-Ikeda, K., Fujiwara, K. & Motokawa, Y. (1999). Eur. J. Biochem. 264, 446-453.
34. Okamura-Ikeda, K., Ohmura, Y., Fujiwara, K. & Motokawa, Y. (1993). Eur. J. Biochem. 216, 539-548.
35. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
36. Pares, S., Cohen-Addad, C., Sieker, L., Neuburger, M. & Douce, R. (1994). Proc. Natl. Acad. Sci. USA, 91, 4850-4853.
37. Ramachandran, G. N. & Sasisekharan, V. (1968). Adv. Protein Chem. 23, 283-438.
38. Toyoda, T., Kobayashi, R., Sekiguchi, T., Koike, K., Koike, M. & Takenaka, A. (1998). Acta Cryst. D54, 982-785.
39. Toyoda, T., Suzuki, K., Sekiguchi, T., Reed, L. J. & Takenaka, A. (1998). J. Biochem. 123, 668-674.
40. Yokoyama, S., Hirota, H., Kigawa, T., Yabuki, T., Shirouzu, M., Terada, T., Ito, Y., Matsuo, Y., Kuroda, Y., Nishimura, Y., Kyogoku, Y., Miki, K., Masui, R. & Kuramitsu, S. (2000). Nature Struct. Biol. 7, 943-945.