The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues

Journal of Biological Chemistry

Volumn 279, Issue 50, 2004, Pages 52255-52261

  Pekkala, Mira ^a   Hieta, Reija ^a   Bergmann, Ulrich ^a   Kivirikko, Kari I ^a   Wierenga, Rik K ^a   Myllyharju, Johanna ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; COLLAGEN; CRYSTAL STRUCTURE; ENZYMES; HYDROXYLATION; MUTAGENESIS; PROTEINS; SYNTHESIS (CHEMICAL);

BINDING SITES; PROTEIN-PROTEIN INTERACTIONS; TETRAMERS; TYROSINES;

ENZYME KINETICS;

GLYCINE; HYDROXYPROLINE; PEPTIDE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROLINE; TETRAMER; TETRATRICOPEPTIDE; TYROSINE; UNCLASSIFIED DRUG;

ALPHA CHAIN; ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CATALYSIS; COLLAGEN SYNTHESIS; CRYSTAL STRUCTURE; HYDROXYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; COLLAGEN; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROCOLLAGEN-PROLINE DIOXYGENASE; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; REPETITIVE SEQUENCES, AMINO ACID; SUBSTRATE SPECIFICITY;

VERTEBRATA;

EID: 10644238913     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M410007200     Document Type: Article

References (50)

1. Kivirikko, K. I., and Pihlajaniemi, T. (1998) Adv. Enzymol. Relat. Areas Mol. Biol. 72, 325-398
2. Kivirikko, K. I., and Myllyharju, J. (1998) Matrix Biol. 16, 357-368
3. Myllyharju, J. (2003) Matrix Biol. 22, 15-24
4. Bruick, R. K., and McKnight, S. L. (2001) Science 294, 1337-1340
5. Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Hetzen, E., Wilson, M. I., Dhanda, A., Tian, Y.-M., Masson, N., Hamilton, D. L., Jaakkola, P., Barstead, R., Hodgkin, J., Maxwell, P. H., Pugh, C. W., Schofield, C. J., and Ratcliffe, P. J. (2001) Cell 107, 43-54
6. Ivan, M., Haberberger, T., Gervasi, D. C., Michelson, K. S., Günzler, V., Kondo, K., Yang, H., Sorokina, I., Conaway, R. C., Conaway, J. W., and Kaelin, W. G., Jr. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 13459-13464
7. Kukkola, L., Hieta, R., Kivirikko, K. I., and Myllyharju, J. (2003) J. Biol. Chem. 278, 47685-47693
8. Van Den Diepstraten, C., Papay, K., Bolender, Z., Brown, A., and Pickering, G. (2003) Circulation 108, 508-511
9. Annunen, P., Autio-Harmainen, H., and Kivirikko, K. I. (1998) J. Biol. Chem. 273, 5989-5992
10. Nissi, R., Autio-Harmainen, H., Marttila, P., Sormunen, R., and Kivirikko, K. I. (2001) J. Histochem. Cytochem. 49, 1143-1153
11. Myllyharju, J., and Kivirikko, K. I. (1997) EMBO J. 16, 1173-1180
12. Myllyharju, J., and Kivirikko, K. I. (2004) Trends Genet. 20, 33-43
13. Myllyharju, J., and Kivirikko, K. I. (1999) EMBO J. 18, 306-312
14. Hieta, R., Kukkola, L., Permi, P., Pirilä, P., Kivirikko, K. I., Kilpeläinen, I., and Myllyharju, J. (2003) J. Biol. Chem. 278, 34966-34974
15. Kay, B., Williamson, M. P., and Sudol, M. (2000) FASEB J. 14, 231-241
16. Macias, M. J., Wiesner, S., and Sudol, M. (2002) FEBS Lett. 513, 30-37
17. Prehoda, K. E., Lee, D. J., and Lim, W. A. (1999) Cell 97, 471-480
18. Ball, L. J., Jarchau, T., Oschkinat, H., and Walter, U. (2002) FEBS Lett. 513, 45-52
19. Freund, C., Kühne, R., Yang, H., Park, S., Reinherz, E. L., and Wagner, G. (2002) EMBO J. 21, 5985-5995
20. Mahoney, N. M., Rozwarski, D. A., Fedorov, E., Fedorov, A. A., and Almo, S. C. (1999) Nat. Struct. Biol. 6, 666-671
21. Nodelman, I. M., Bowman, G. D., Lindberg, U., and Schutt, C. (1999) J. Mol. Biol. 294, 1271-1285
22. Pornillos, O., Alam, S. L., Davis, D. R., and Sundquist, W. I. (2002) Nat. Struct. Biol. 9, 812-817
23. Pekkala, M., Hieta, R., Kursula, P., Kivirikko, K. I., Wierenga, R. K., and Myllyharju, J. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 940-942
24. Main, E. R. G., Xiong, Y., Cocco, M. J., D'Andrea, L., and Regan, L. (2003) Structure 11, 497-508
25. D'Andrea, L. D., and Regan, L. (2003) Trends Biochem. Sci. 28, 655-662
26. Gatto, G. J., Jr., Geisbrecht, B. V., Gould, S. J., and Berg, J. M. (2000) Nat. Struct. Biol. 7, 1091-1095
27. Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., and Moarefi, I. (2000) Cell 101, 199-210
28. Kivirikko, K. I., and Myllylä, R. (1982) Methods Enzymol. 82, 245-304
29. Myllylä, R., Tuderman, L., and Kivirikko, K. I. (1977) Eur. J. Biochem. 80, 349-357
30. Kabsch, W. (1988) J. Appl. Crystallogr. 21, 916-924
31. Collaborative Computational Project, Number 4 (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
32. Terwilliger, T. C., and Berendzen, J. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 849-861
33. Jones, A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sect. A 47, 110-119
34. McRee, D. E. (1999) J. Struct. Biol. 125, 156-165
35. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. Sect. D Biol. Crystallogr. 53, 240-255
36. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
37. Abagyan, R. A., Totrov, M. M., and Kuznetsov, D. N. (1994) J. Comput. Chem. 15, 488-506
38. Holm, L., and Sander, C. (1997) Nucleic Acids Res. 25, 231-234
39. Kabsch, W., and Sander, C. (1983) Biopolymers 22, 2577-2637
40. Bella, J., Eaton, M., Brodsky, B., and Berman, H. M. (1994) Science 266, 75-81
41. Berisio, R., Vitagliano, L., Mazzarella, L., and Zagari, A. (2002) Protein Sci. 11, 262-270
42. Jenkins, C. L., and Raines, R. T. (2002) Nat. Prod. Rep. 19, 49-59
43. Rucker, A. L., Pager, C. T., Campbell, M. N., Quails, J. E., and Creamer, T. P. (2003) Proteins 53, 68-75
44. Zarrinpar, A., Bhattacharyya, R. P., and Lim, W. A. (2003) Science's STKE, www.stke.org/cgi/content/full/sigtrans;2003/179/re8
45. Zarrinpar, A., and Lim, W. A. (2000) Nat. Struct. Biol. 7, 611-613
46. Bhattacharyya, R., and Chakrabarti, P. (2003) J. Mol. Biol. 331, 925-940
47. Kemmink, J., Darby, N. J., Dijkstra, K., Nilges, M., and Creighton, T. E. (1996) Biochemistry 35, 7684-7691
48. Kemmink, J., Darby, N. J., Dijkstra, K., Nilges, M., and Creighton, T. E. (1997) Curr. Biol. 7, 239-245
49. Dijkstra, K., Karvonen, P., Pirneskoski, A., Koivunen, P., Kivirikko, K. I., Darby, N. J., van Straaten, M., Scheek, R. M., and Kemmink, J. (1999) J. Biomol. NMR 14, 195-196
50. Atreya, P. L., and Ananthanarayanan, V. S. (1991) J. Biol. Chem. 266, 2852-2858