The crystal structure of progesterone 5β-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases

Journal of Biological Chemistry

Volumn 283, Issue 25, 2008, Pages 17260-17269

  Thorn, Andrea ^a   Egerer Sieber, Claudia ^a   Jäger, Christof M ^a   Herl, Vanessa ^a   Müller Uri, Frieder ^a   Kreis, Wolfgang ^a   Muller, Yves A ^a  

^a UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; BIOSYNTHETIC PATHWAYS; CATALYTIC RESIDUES; COFACTOR; CONJUGATED DOUBLE BONDS; ENZYMATIC ACTIVITIES; KEY ENZYMES; LYSINE RESIDUES; PLANT ENZYMES; SEQUENCE MOTIFS; STEREOSPECIFIC REDUCTIONS; STEROID SUBSTRATES; TERNARY COMPLEXES;

AMINO ACIDS; ENZYMES; INFORMATION RETRIEVAL; MODEL STRUCTURES; PROTEINS;

CRYSTAL STRUCTURE;

ALANINE; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PHENYLALANINE; PROGESTERONE; PROGESTERONE 5BETA REDUCTASE; TYROSINE; UNCLASSIFIED DRUG; 3BETA HYDROXY DELTA5 STEROID DEHYDROGENASE; DIGITALIS; RECOMBINANT PROTEIN;

ADDITION REACTION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; COVALENT BOND; CRYSTAL STRUCTURE; DIGITALIS LANATA; ENZYME ACTIVE SITE; ENZYME ACTIVITY; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN MOTIF; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; BINDING SITE; BIOLOGICAL MODEL; CHEMISTRY; CONFORMATION; ENZYME SPECIFICITY; KINETICS; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); DIGITALIS (GENUS); DIGITALIS LANATA;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIGITALIS; KINETICS; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES; PROGESTERONE REDUCTASE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 47749101233     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M706185200     Document Type: Article

References (52)

1. Withering, W. (1941) in Classics of Cardiology (Williams, F. A., and Keys, T. E., eds) pp. 231-252, Dover Publications, New York
2. Gheorghiade, M., Adams, K. F., Jr., and Colucci, W. S. (2004) Circulation 109, 2959-2964
3. Antman, E. M., and Smith, T. W. (1985) Annu. Rev. Med. 36, 357-367
4. Mathews, C. K., van Holde, K. E., and Ahern, K. G. (2000) Biochemistry, pp. 340-342, 3rd Ed., Addison-Wesley Publishing Co., San Francisco
5. Herl, V., Fischer, G., Muller-Uri, F., and Kreis, W. (2006) Phytochemistry 67, 225-231
6. Gärtner, D. E., Wendroth, S., and Seitz, H. U. (1990) FEBS Lett. 271, 239-242
7. Caspi, E., and Lewis, D. O. (1967) Science 156, 519-520
8. Jez, J. M., and Penning, T. M. (2001) Chem. Biol. Interact. 130-132, 499-525
9. Rossman, M. G., Liljas, A., Branden, C.-I., and Banaszak, L. J. (1975) in The Enzymes (Boyer, P. D., ed) 3rd Ed., pp. 61-102, Academic Press, New York
10. Kallberg, Y., Oppermann, U., Jornvall, H., and Persson, B. (2002) Eur. J. Biochem. 269, 4409-4417
11. Jornvall, H., Persson, B., Krook, M., Atrian, S., Gonzalez-Duarte, R., Jeffery, J., and Ghosh, D. (1995) Biochemistry 34, 6003-6013
12. Edwards, K. J., Barton, J. D., Rossjohn, J., Thorn, J. M., Taylor, G. L., and Ollis, D. L. (1996) Arch. Biochem. Biophys. 328, 173-183
13. Jornvall, H., Hoog, J. O., and Persson, B. (1999) FEBS Lett. 445, 261-264
14. Jornvall, H., Persson, B., and Jeffery, J. (1987) Eur. J. Biochem. 167, 195-201
15. Kallberg, Y., Oppermann, U., Jornvall, H., and Persson, B. (2002) Protein Sci. 11, 636-641
16. Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) J. Mol. Biol. 247, 536-540
17. Webb, N. A., Mulichak, A. M., Lam, J. S., Rocchetta, H. L., and Garavito, R. M. (2004) Protein Sci. 13, 529-539
18. Persson, B., Kallberg, Y., Oppermann, U., and Jornvall, H. (2003) Chem. Biol. Interact. 143-144, 271-278
19. Filling, C., Berndt, K. D., Benach, J., Knapp, S., Prozorovski, T., Nordling, E., Ladenstein, R., Jornvall, H., and Oppermann, U. (2002) J. Biol. Chem. 277, 25677-25684
20. Bennett, M. J., Schlegel, B. P., Jez, J. M., Penning, T. M., and Lewis, M. (1996) Biochemistry 35, 10702-10711
21. Gavidia, I., Tarrio, R., Rodriguez-Trelles, F., Perez-Bermudez, P., and Seitz, H. U. (2006) Phytochemistry 68, 853-864
22. Penning, T. M., Ma, H., and Jez, J. M. (2001) Chem. Biol. Interact. 130-132, 659-671
23. Egerer-Sieber, C., Herl, V., Muller-Uri, F., Kreis, W., and Muller, Y. A. (2006) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62, 186-188
24. Stuhlemmer, U., and Kreis, W. (1996) Plant Physiol. Biochem. 34, 85-91
25. Chayen, N. E. (1996) Protein Eng. 9, 927-929
26. Kabsch, W. (1988) J. Appl. Crystallogr. 21, 916-924
27. Brunger, A. T. (1993) Acta Crystallogr. Sect. D Biol. Crystallogr. 49, 24-36
28. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. Sect. D Biol. Crystallogr. 60, 2126-2132
29. Read, R. J. (1986) Acta Crystallogr. Sect. A 42, 140-149
30. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. Sect. D Biol. Crystallogr. 53, 240-255
31. Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Acta Crystallogr. Sect. D Biol. Crystallogr. 57, 122-133
32. Stiebritz, M. T., and Muller, Y. A. (2006) Acta Crystallogr. Sect. D Biol. Crystallogr. 62, 648-658
33. Dunbrack, R. L., Jr., and Cohen, F. E. (1997) Protein Sci. 6, 1661-1681
34. Lazaridis, T., and Karplus, M. (1999) Proteins 35, 133-152
35. Kortemme, T., Morozov, A. V., and Baker, D. (2003) J. Mol. Biol. 326, 1239-1259
36. Leach, A. R. (1994) J. Mol. Biol. 235, 345-356
37. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
38. Rossman, M. G., and Argos, P. (1976) J. Mol. Biol. 105, 75-95
39. Holm, L., and Sander, C. (1995) Trends Biochem. Sci. 20, 478-480
40. Berman, H. M., Battistuz, T., Bhat, T. N., Bluhm, W. F., Bourne, P. E., Burkhardt, K., Feng, Z., Gilliland, G. L., Iype, L., Jain, S., Fagan, P., Marvin, J., Padilla, D., Ravichandran, V., Schneider, B., Thanki, N., Weissig, H., Westbrook, J. D., and Zardecki, C. (2002) Acta Crystallogr. Sect. D Biol. Crystallogr. 58, 899-907
41. Bottoms, C. A., Smith, P. E., and Tanner, J. J. (2002) Protein Sci. 11, 2125-2137
42. Major, L. L., Wolucka, B. A., and Naismith, J. H. (2005) J. Am. Chem. Soc. 127, 18309-18320
43. Grimm, C., Maser, E., Mobus, E., Klebe, G., Reuter, K., and Ficner, R. (2000) J. Biol. Chem. 275, 41333-41339
44. Breton, R., Housset, D., Mazza, C., and Fontecilla-Camps, J. C. (1996) Structure (Lond.) 4, 905-915
45. Parikh, S., Moynihan, D. P., Xiao, G., and Tonge, P. J. (1999) Biochemistry 38, 13623-13634
46. Jez, J. M., and Penning, T. M. (1998) Biochemistry 37, 9695-9703
47. Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Nucleic Acids Res. 25, 3389-3402
48. Rafferty, J. B., Simon, J. W., Baldock, C., Artymiuk, P. J., Baker, P. J., Stuitje, A. R., Slabas, A. R., and Rice, D. W. (1995) Structure (Lond.) 3, 927-938
49. Bjorkhem, I., Buchmann, M., and Bystrom, S. (1992) J. Biol. Chem. 267, 19872-19875
50. Alphey, M. S., Yu, W., Byres, E., Li, D., and Hunter, W. N. (2005) J. Biol. Chem. 280, 3068-3077
51. Ghosh, D., Weeks, C. M., Grochulski, P., Duax, W. L., Erman, M., Rimsay, R. L., and Orr, J. C. (1991) Proc. Natl. Acad. Sci. U. S. A. 88, 10064-10068
52. Wallace, A. C., Laskowski, R. A., and Thornton, J. M. (1995) Protein Eng. 8, 127-134