Structure-function analysis of the endoplasmic reticulum oxidoreductase TMX3 reveals interdomain stabilization of the N-terminal redox-active domain

Journal of Biological Chemistry

Volumn 282, Issue 46, 2007, Pages 33859-33867

  Haugstetter, Johannes ^a   Maurer, Michael Andreas ^a   Blicher, Thomas ^b   Pagac, Martin ^a,c   Wider, Gerhard ^a   Ellgaard, Lars ^a,d  

^a ETH ZURICH   (Switzerland)

^b TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^c UNIVERSITY OF FRIBOURG   (Switzerland)

^d UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; ENZYME KINETICS; PROTEOLYSIS; REDOX REACTIONS;

PROTEIN DISULFIDE-ISOMERASE; THIOL-DISULFIDE OXIDOREDUCTASE;

MOLECULAR STRUCTURE;

OXIDOREDUCTASE;

AMINO TERMINAL SEQUENCE; ARTICLE; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; HUMAN; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BINDING SITES; ENDOPLASMIC RETICULUM; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 36348948649     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M706442200     Document Type: Article

References (43)

1. Givol, D., Goldberger, R. F., and Anfinsen, C. B. (1964) J. Biol. Chem. 239, PC3114-3116
2. Creighton, T. E., Hillson, D. A., and Freedman, R. B. (1980) J. Mol. Biol. 142, 43-62
3. Weissman, J. S., and Kim, P. S. (1993) Nature 365, 185-188
4. Darby, N. J., Freedman, R. B., and Creighton, T. E. (1994) Biochemistry 33, 7937-7947
5. Ellgaard, L., and Ruddock, L. W. (2005) EMBO Rep. 6, 28-32
6. Sevier, C. S., and Kaiser, C. A. (2006) Antioxid. Redox. Signal. 8, 797-811
7. Klappa, P., Ruddock, L. W., Darby, N. J., and Freedman, R. B. (1998) EMBO J. 17, 927-935
8. Russell, S. J., Ruddock, L. W., Salo, K. E., Oliver, J. D., Roebuck, Q. P., Llewellyn, D. H., Roderick, H. L., Koivunen, P., Myllyharju, J., and High, S. (2004) J. Biol. Chem. 279, 18861-18869
9. Kozlov, G., Maattanen, P., Schrag, J. D., Pollock, S., Cygler, M., Nagar, B., Thomas, D. Y., and Gehring, K. (2006) Structure 14, 1331-1339
10. Alanen, H. I., Salo, K. E., Pirneskoski, A., and Ruddock, L. W. (2006) Antioxid. Redox. Signal. 8, 283-291
11. Darby, N. J., and Creighton, T. E. (1995) Biochemistry 34, 11725-11735
12. Darby, N. J., Penka, E., and Vincentelli, R. (1998) J. Mol. Biol. 276, 239-247
13. Frickel, E. M., Frei, P., Bouvier, M., Stafford, W. F., Helenius, A., Glockshuber, R., and Ellgaard, L. (2004) J. Biol. Chem. 279, 18277-18287
14. Tian, G., Xiang, S., Noiva, R., Lennarz, W. J., and Schindelin, H. (2006) Cell 124, 61-73
15. Jessop, C. E., Chakravarthi, S., Garbi, N., Hämmerling, G. J., Lovell, S., and Bulleid, N. J. (2007) EMBO J. 26, 28-40
16. Meng, X., Zhang, C., Chen, J., Peng, S., Cao, Y., Ying, K., Xie, Y., and Mao, Y. (2003) Biochem. Genet. 41, 99-106
17. Matsuo, Y., Akiyama, N., Nakamura, H., Yodoi, J., Noda, M., and Kizaka-Kondoh, S. (2001) J. Biol. Chem. 276, 10032-10038
18. Matsuo, Y., Nishinaka, Y., Suzuki, S., Kojima, M., Kizaka-Kondoh, S., Kondo, N., Son, A., Sakakura-Nishiyama, J., Yamaguchi, Y., Masutani, H., Ishii, Y., and Yodoi, J. (2004) Arch. Biochem. Biophys. 423, 81-87
19. Haugstetter, J., Blicher, T., and Ellgaard, L. (2005) J. Biol. Chem. 280, 8371-8380
20. Appenzeller-Herzog, C., and Ellgaard, L. (2007) Antiox. Redox. Signal., 10, 10.1089/ars.2007.1837
21. Zahn, R., Buckle, A. M., Perrett, S., Johnson, C. M., Corrales, F. J., Golbik, R., and Fersht, A. R. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 15024-15029
22. Gill, S. C., and von Hippel, P. H. (1989) Anal. Biochem. 182, 319-326
23. Kumar, A., Ernst, R. R., and Wuthrich, K. (1980) Biochem. Biophys. Res. Commun. 95, 1-6
24. Bodenhausen, G., and Ruben, D. J. (1980) Chem. Phys. Lett. 69, 185-189
25. Monsellier, E., and Bedouelle, H. (2005) Protein. Eng. Des. Sel. 18, 445-456
26. Ruddock, L. W., Hirst, T. R., and Freedman, R. B. (1996) Biochem. J. 315, 1001-1005
27. Hansen, R. E., Ostergaard, H., and Winther, J. R. (2005) Biochemistry 44, 5899-5906
28. Sali, A., and Blundell, T. L. (1993) J. Mol. Biol. 234, 779-815
29. Kemmink, J., Darby, N. J., Dijkstra, K., Nilges, M., and Creighton, T. E. (1996) Biochemistry 35, 7684-7691
30. Wang, S., Trumble, W. R., Liao, H., Wesson, C. R., Dunker, A. K., and Kang, C. H. (1998) Nat. Struct. Biol. 5, 476-483
31. Wallner, B., and Elofsson, A. (2003) Protein Sci. 12, 1073-1086
32. Davis, I. W., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2004) Nucleic Acids Res. 32, W615-W619
33. Rost, B., Yachdav, G., and Liu, J. (2004) Nucleic Acids Res. 32, W321-W326
34. Qin, J., Clore, G. M., Kennedy, W. M., Huth, J. R., and Gronenborn, A. M. (1995) Structure 3, 289-297
35. Maeda, K., Hagglund, P., Finnie, C., Svensson, B., and Henriksen, A. (2006) Structure 14, 1701-1710
36. Martin, J. L., Bardwell, J. C., and Kuriyan, J. (1993) Nature 365, 464-468
37. Darby, N. J., and Creighton, T. E. (1995) Biochemistry 34, 16770-16780
38. Raturi, A., and Mutus, B. (2007) Free Radic. Biol. Med. 43, 62-70
39. Alanen, H. I., Salo, K. E., Pekkala, M., Siekkinen, H. M., Pirneskoski, A., and Ruddock, L. W. (2003) Antioxid. Redox Signal 5, 367-374
40. Zapun, A., Bardwell, J. C., and Creighton, T. E. (1993) Biochemistry 32, 5083-5092
41. Mezghrani, A., Fassio, A., Benham, A., Simmen, T., Braakman, I., and Sitia, R. (2001) EMBO J. 20, 6288-6296
42. Lappi, A. K., Lensink, M. F., Alanen, H. I., Salo, K. E., Lobell, M., Juffer, A. H., and Ruddock, L. W. (2004) J. Mol. Biol. 335, 283-295
43. Delano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific, Palo Alto, CA