Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 66, Issue 6, 2010, Pages 738-743

  Merli, Angelo ^a   Manikandan, Karuppasamy ^b   Graczer V ^c   Schuldt, Linda ^b   Singh, Rajesh Kumar ^d   Závodszky, Péter ^c   Vas, Mária ^c   Weiss, Manfred S ^b,e  

^a UNIVERSITY OF PARMA   (Italy)

^b DESY   (Germany)

^c INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^d NATIONAL CHEMICAL LABORATORY   (India)

^e HAHN MEITNER INSTITUT   (Germany)

Author keywords

Isopropylmalate dehydrogenase; Leucine biosynthesis pathway; Thermus thermophilus

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

3-ISOPROPYLMALATE DEHYDROGENASE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; SUBSTRATE SPECIFICITY; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 77953153404     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S174430911001626X     Document Type: Article

References (24)

1. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D 50, 760-763.
2. Dean, A. M. & Dvorak, L. (1995). Protein Sci. 4, 2156-2167.
3. French, S. & Wilson, K. (1978). Acta Cryst. A 34, 517-525.
4. Gerstein, M. & Echols, N. (2004). Curr. Opin. Chem. Biol. 8, 14-19.
5. Gráczer, É., Varga, A., Hajdú, I., Melnik, B., Szilágyi, A., Semisotnov, G., Závodszky, P. & Vas, M. (2007). Biochemistry, 46, 11536-11549.
6. Hayashi-Iwasaki, Y. & Oshima, T. (2000). Methods Enzymol. 324, 301-322.
7. Hayward, S. (2004). J. Mol. Biol. 339, 1001-1021.
8. Hurley, J. H. & Dean, A. M. (1994). Structure, 2, 1007-1016.
9. Hurley, J. H., Dean, A. M., Koshland, D. E. Jr & Stroud, R. M. (1991). Biochemistry, 30, 8671-8678.
10. Imada, K., Inagaki, K., Matsunami, H., Kawaguchi, H., Tanaka, H., Tanaka, N. & Namba, K. (1998). Structure, 6, 971-982.
11. Imada, K., Sato, M., Tanaka, N., Katsube, Y., Matsuura, Y. & Oshima, T. (1991). J. Mol. Biol. 222, 725-738.
12. Kadono, S., Sakurai, M., Moriyama, H., Sato, M., Hayashi, Y., Oshima, T. & Tanaka, N. (1995). J. Biochem (Tokyo), 118, 745-752.
13. Katsube, Y., Tanaka, N., Takenaka, A., Yamada, T. & Oshima, T. (1988). J. Biochem. 104, 679-680.
14. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
15. Nagata, C., Moriyama, H., Tanaka, N., Nakasako, M., Yamamoto, M., Ueki, T. & Oshima, T. (1996). Acta Cryst. D 52, 623-630.
16. Nango, E., Yamamoto, T., Kumasaka, T. & Eguchi, T. (2009). Bioorg. Med. Chem. 17, 7789-7794.
17. Németh, A., Svingor, A., Pocsik, M., Dobó, J., Magyar, C., Szilágyi, A., Gál, P. & Závodszky, P. (2000). FEBS Lett. 468, 48-52.
18. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
19. Sakurai, M., Onodera, K., Moriyama, H., Matsumoto, O., Tanaka, N., Numata, K., Imada, K., Sato, M., Katsube, Y. & Oshima, T. (1992). J. Biochem. 112, 173-174.
20. Singh, R. K., Kefala, G., Janowski, R., Mueller-Dieckmann, C., von Kries, J. P. & Weiss, M. S. (2005). J. Mol. Biol. 346, 1-11.
21. Tsuchiya, D., Sekiguchi, T. & Takenaka, A. (1997). J. Biochem. (Tokyo), 122, 1092-1104.
22. Vaguine, A. A., Richelle, J. & Wodak, S. J. (1999). Acta Cryst. D 55, 191-205.
23. Wallon, G., Kryger, G., Lovett, S. T., Oshima, T., Ringe, D. & Petsko, G. A. (1997). J. Mol. Biol. 266, 1016-1031.
24. Weiss, M. S. (2001). J. Appl. Cryst. 34, 130-135.