Structure of Chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L-threo-tetrahydrobiopterin

Journal of Biological Chemistry

Volumn 281, Issue 4, 2006, Pages 2249-2256

  Supangat, Supangat ^a   Kyung, Hye Seo ^a   Yong, Kee Choi ^b   Young, Shik Park ^b   Son, Daeyoung ^a   Han, Chang Deok ^a   Kon, Ho Lee ^a  

^a Gyeongsang National University   (South Korea)

^b Inje University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AROMATIC COMPOUNDS; BIOSYNTHESIS; COMPLEXATION; REACTION KINETICS; SUBSTRATES;

ANIMAL ENZYMES; CHLOROBIUM TEPIDUM SEPIAPTERIN; SEPIAPTERIN REDUCTASE (SR); TETRAHYDROBIOPTERIN;

PROTEINS;

NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SEPIAPTERIN; SEPIAPTERIN REDUCTASE; TETRAHYDROBIOPTERIN; THREO TETRAHYDROBIOPTERIN; UNCLASSIFIED DRUG; 5,6,7,8-TETRAHYDROBIOPTERIN; ALCOHOL DEHYDROGENASE; BIOPTERIN; DRUG DERIVATIVE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; BINDING AFFINITY; BINDING SITE; BIOSYNTHESIS; CATALYSIS; CHLOROBIUM; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE ALIGNMENT; STEREOSPECIFICITY; ANIMAL; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; ESCHERICHIA COLI; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; MOUSE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STEREOISOMERISM; X RAY CRYSTALLOGRAPHY;

ANIMALIA; CHLOROBACULUM TEPIDUM;

ALCOHOL OXIDOREDUCTASES; ANIMALS; BINDING SITES; BIOPTERIN; CATALYTIC DOMAIN; CHLOROBIUM; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; MICE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADP; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STEREOISOMERISM;

EID: 33644869409     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M509343200     Document Type: Article

References (39)

1. Kaufman, S. (1993) Annu. Rev. Nutr. 13, 261-286
2. Marletta, M. A. (1994) Cell 78, 927-930
3. Thöny, B., Auerbach, G., and Blau, N. (2000) Biochem. J. 347, 1-16
4. Werner-Felmayer, G., Golderer, G., and Werner, E. R. (2002) Curr. Drug Metab. 3, 159-173
5. Blau, N., Bonafe, L., and Thöny, B. (2001) Mol. Genet. Metab. 74, 172-185
6. Katoh, S., and Sueoka, T. (1987) J. Biochem. (Tokyo) 101, 275-278
7. Katoh, S., and Sueoka, T. (1988) J. Biochem. (Tokyo) 103, 286-289
8. Auerbach, G., Herrmann, A., Gutlich, M., Fischer, M., Jacob, U., Bacher, A., and Huber, R. (1997) EMBO J. 16, 7219-7230
9. Milstien, S., and Kaufman, S. (1989) Biochem. Biophys. Res. Commun. 165, 845-850
10. Park, Y. S., Heizmann, C. W., Wermuth, B., Levine, R. A., Steinerstauch, P., Guzman, J., and Blau, N. (1991) Biochem. Biophys. Res. Commun. 175, 738-744
11. Bonafe, L., Thony, B., Penzien, J. M., Czarnecki, B., and Blau, N. (2001) Am. J. Hum. Genet. 69, 269-277
12. Klein, R., Thiery, R., and Tatischeff, I. (1990) Eur. J. Biochem. 187, 665-669
13. Cho, S. H., Na, J. U., Youn, H., Hwang, C. S., Lee, C. H., and Kang, S. O. (1998) Biochim. Biophys. Acta 1379, 53-60
14. Cho, S. H., Na, J. U., Youn, H., Hwang, C. S., Lee, C. H., and Kang, S. O. (1999) Biochem. J. 340, 497-503
15. Choi, Y. K., Jun, S. R., Cha, E. Y., Park, J. S., and Park, Y. S. (2005) FEMS Microbiol. Lett. 242, 95-99
16. Kim, Y. A., Chung, H. J., Kim, Y. J., Choi, Y. K., Hwang, Y. K., Lee, S. W., and Park, Y. S. (2000) Mol. Cell 10, 405-410
17. Choi, Y. K., Park, J. S., Kong, J. S., Morio, T., and Park, Y. S. (2005) FEBS Lett. 579, 3085-3089
18. Supangat, S., Choi, Y. K., Young, S. P., Son, D., Han, C. D., and Lee, K. H. (2005) Acta Crystallogr. F 61, 202-204
19. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
20. Hendrickson, W. A. (1991) Science 254, 51-58
21. CCP4 (1994) Acta Crystallogr. D 50, 760-763
22. Terwilliger, T. C., and Berendzen, J. (1999) Acta Crystallogr. D 55, 1872-1877
23. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. A 47, 110-119
24. 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., and Warren, G. L. (1998) Acta Crystallogr. D 54, 905-921
25. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
26. DeLano, W. L. (2001) The pyMol Molecular Graphics System, DeLano Scientific, San Carlos, CA
27. Gouet, P., Courcelle, E., Stuart, D. I., and Metoz, F. (1999) Bioinformatics 15, 305-308
28. Ghosh, D., Wawrzak, Z., Weeks, C. M., Duax, W. L., and Erman, M. (1994) Structure 2, 629-640
29. Rossmann, M. G., Liljas, A., Bränden, C.-I., and Banaszak, L. J. (1975) The Enzymes, pp. 61-102, Academic Press, Inc., New York
30. Holm, L., and Sander, C. (1995) Trends Biochem. Sci. 20, 478-480
31. Tanaka, N., Nonaka, T., Nakanishi, M., Deyashiki, Y., Hara, A., and Mitsui, Y. (1996) Structure 4, 33-45
32. Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzalez-Duarte, R., Jeffery, J., and Ghosh, D. (1995) Biochemistry 34, 6003-6013
33. Fujimoto, K., Hara, M., Yamada, H., Sakurai, M., Inaba, A., Tomomura, A., and Katoh, S. (2001) Chem. Biol. Interact. 130-132, 825-832
34. Katoh, S., and Sueoka, T. (1984) Biochem. Biophys. Res. Commun. 118, 859-866
35. Smith, G. K. (1987) Arch. Biochem. Biophys. 255, 254-266
36. Nakajima, K., Yamashita, A., Akama, H., Nakatsu, T., Kato, H., Hashimoto, T., Oda, J., and Yamada, Y. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 4876-4881
37. Nakajima, K., Kato, H., Oda, J., Yamada, Y., and Hashimoto, T. (1999) J. Biol. Chem. 274, 16563-16568
38. Kabsch, W., and Sander, C. (1983) Biopolymers 22, 2577-2637
39. Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) Nucleic Acids Res. 25, 4876-4882