Crystal structure of lodotyrosine deiodinase, a novel flavoprotein responsible for lodide salvage in thyroid glands

Journal of Biological Chemistry

Volumn 284, Issue 29, 2009, Pages 19659-19667

  Thomas, Seth R ^a,b   McTamney, Patrick M ^a   Adler, Jennifer M ^a   LeRonde LeBlanc, Nicole ^a,b   Rokita, Steven E ^a  

^a Bldg 142   (United States)

^b UNIVERSITY OF MARYLAND   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CARBON-IODINE BONDS; CATALYTIC BEHAVIOR; CO-CRYSTALS; ELECTRON TRANSFER; FLAVIN MONONUCLEOTIDE; HYDROGEN BONDINGS; MEMBRANE-BOUND ENZYMES; MOLECULAR BASIS; SOLUBLE DOMAINS; THYROID DISEASE; THYROID GLANDS; THYROID HORMONES; VITAMIN B;

BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; COORDINATION REACTIONS; CRYSTAL STRUCTURE; ENZYMES; HYDROGEN; HYDROGEN BONDS; IODINE; SALVAGING;

SUBSTRATES;

DIIODOTYROSINE; ENZYME; FLAVOPROTEIN; IODIDE PEROXIDASE; IODOTYROSINE; PROTEIN BLUB; QUERCETIN; UNCLASSIFIED DRUG; CARBON; FLAVINE MONONUCLEOTIDE; IODIDE; IODINE;

ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; THYROID GLAND; ANIMAL; ARMYWORM; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; GENETICS; METABOLISM; MOUSE; MUTATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; X RAY DIFFRACTION;

ANIMALS; BINDING SITES; CARBON; CELL LINE; CRYSTALLIZATION; DIIODOTYROSINE; FLAVIN MONONUCLEOTIDE; IODIDE PEROXIDASE; IODIDES; IODINE; MICE; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SPODOPTERA; SUBSTRATE SPECIFICITY; THYROID GLAND; X-RAY DIFFRACTION;

EID: 67749120727     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.013458     Document Type: Article

References (48)

1. Moreno, J. C., Klootwijk, W., van Toor, H., Pinto, G., D'Alessandro, M., Léger, A., Goudie, D., Polak, M., Grüters, A., and Visser, T. J. (2008) N Engl. J. Med. 358, 1811-1818
2. Dohán, O., De la Vieja, A., Paroder, V., Riedel, C., Artani, M., Reed, M. Ginter, C. S., and Carrasco, N. (2003) Endocr. Rev. 24, 48-77
3. Gnidehou, S., Caillou, B., Talbot, M., Ohayon, R., Kaniewski, I., Noël-Hudson, M. S., Morand, S., Agnangji, D., Sezan, A., Courtin, F., Virion, A. and Dupuy, C. (2004) FASEB J. 18, 1574-1576
4. Friedman, I. E., Watson, J. A., Jr., Lam, D. W., and Rokita, S. E. (2006) J. Biol. Chem. 281, 2812-2819
5. Bianco, A. C., Salvatore, D., Gereben, B., Berry, M. J., and Larsen, P. R (2002) Endocr. Rev. 23, 38-89
6. Watson, J. A., Jr., McTarrmey, P. M., Adler, J. M., and Rokita, S. E. (2008) ChemBioChem 9, 504-506
7. Goswami, A., and Rosenberg, I. N. (1979) J. Biol. Chem. 254, 12326-12330
8. De Colibus, L., and Mattevi, A. (2006) Curr. Opin. Struct. Biol. 16, 722-728
9. Joosten, V., and van Berkel, W. J. (2007) Curr. Opin. Chem. Biol. 11, 195-202
10. Mansoorabadi, S. O., Thibodeaux, C. J., and Liu, H. W. (2007) J. Org. Chem. 72, 6329-6342
11. van Pée, K. H., and Patallo, E. P. (2006) Appl. Microbiol. Biotechnol. 70, 631-641
12. Suzuki, T., and Kasia, N. (2003) Trends Glycosci. Glycotechnol. 15, 329-349
13. O'Reilly, D. R., Miller, L. K., and Luckow, V. A. (1994) Baculovirus Expression Vectors: a Laboratory Manual, pp. 130-134, Oxford University Press, Inc., New York
14. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
15. Pape, T., and Schneider, T. R. (2004) J. Appl. Crystallogr. 37, 843-844
16. Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Nat Struct. Biol. 6, 458-463
17. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. D Biol. Crystallogr. 53, 240-255
18. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
19. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., and Read. R. J. (2007) J. Appl. Crystallogr. 40, 658-674
20. Collaborative. (1994) Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
21. Tu, S. C. (2001) Antioxid Redox Signal 3, 881-897
22. Holm, L., and Park, J. (2000) Bioinformatics 16, 566-567
23. Taga, M. E., Larsen, N. A., Howard-Jones, A. R., Walsh, C. T., and Walker, G. C. (2007) Nature 446, 449-453
24. Metrangolo, P., Meyer, F., Pilati, T., Resnati, G., and Terraneo, G. (2008) Angew. Chem. Int. Ed. Engl, 447, 6114-6127
25. Matter, H., Nazaré, M., Güsregen, S., Will, D. W., Schreuder, H., Bauer, A., Urmann, M., Ritter, K., Wagner, M., and Wehner, V. (2009) Angew. Chem. Int. Ed. Engl. 49, 2911-2916
26. Auffinger, P., Hays, F. A., Westhof, E., and Ho, P. S. (2004) Proc. Natl. Acad. Sci., U.S.A. 101, 16789-16794
27. Cody, V., and Murray-Rust, P. (1984) J. Mcl. Struct. 112, 189-199
28. Gales, L., Mácedo-Ribeiro, S., Arsequell, G., Valencia, G., Saratva, M. J., and Damas, A. M. (2005) Biochem. J. 388, 615-621
29. Parkinson, G. T., Skelly, J. V. and Neidle, S. (2000) J. Med. Chem. 43, 3624-3631
30. Fraaije, M. W., and Mattevi, A. (2000) Trends Biochem Sci. 25, 126-132
31. Legrand, Y. M., Gray, M., Cooke, G., and Rotello, V. M. (2003) J. Am. Chem Soc. 125, 15780-15795
32. Lyubimov, A. Y., Lario, P. I., Moustafa, I., and Vrielink, A. (2006) Nat. Chem. Biol. 2, 259-264
33. Tanner, J. J., Lei, B., Tu, S. C., and Krause, K. L. (1996) Biochemistry 35, 13531-13539
34. Haynes, C. A., Koder, R. L., Miller, A. F., and Rodgers, D. W. (2002) J. Biol. Chem. 277, 11513-11520
35. Hecht, H. J., Erdmann, H., Park, H. J., Sprinzl, M., and Schmid, R. D. (1995) Nat. Struct. Biol. 2, 1109-1114
36. Koike, H., Sasaki, H., Kobori, T., Zenno, S., Saigo, K., Murphy, M. E., Adman, E. T., and Tanokura, M. (1998) J. Mol, Biol. 280, 259-273
37. Kobori, T., Sasaki, H., Lee, W. C., Zenno, S., Saigo, K., Murphy, M. E., and Tanokura, M. (2001) J. Biol. Chem. 276, 2816-2823
38. Lovering, A. L., Hyde, E. I., Searle, P. F., and White, S. A. (2001) J. Mol. Biol, 309, 203-213
39. Johansson, E., Parkinson, G. N., Denny, W. A., and Neidle, S. (2003) J. Med. Chem. 46, 4009-4020
40. Tanner, J. J., Tu, S. C., Barbour, L. J., Barnes, C. L., and Krause, K. L. (1999) Protein Sci. 8, 1725-1732
41. Goswami, A., and Rosenberg, I. N. (1977) Endocrinology 101, 331-341
42. Solís-S., J. C., Villalobos, P., Orozco, A., and Valverde-R., C. (2004) J. Endocrinol. 181, 385-392
43. Yang, K. Y., and Swanson, R. P. (2007) Biochemistry 46, 2289-2297
44. Thorpe, C., and Kim, J. J. (1995) FASEB J. 9, 718-725
45. Vock, P., Engst, S., Eder, M., and Ghisla, S. (1998) Biochemistry 37, 1848-1860
46. Kunishima, M., Friedman, J. E., and Rokita, S. E. (1999) J. Am. Chem. Soc. 121, 4722-4723
47. Delano,W. (2002) PyMOL, Delano Scientific, San Carlos, CA
48. Afink, G., Kulik, W., Overmars, H., de Randamie, J., Veenboer, T, van Cruchten, A., Craen, M., and Ris-Stalpers, C. (2008) J. Clin. Endocrinol. Metab. 93, 4894-4901