Crystal structure of paprika ferredoxin-NADP+ reductase: Implications for the electron transfer pathway

Journal of Biological Chemistry

Volumn 276, Issue 12, 2001, Pages 9253-9263

  Dorowski, Anja ^a   Hofmann, Andreas ^a,b   Steegborn, Clemens ^a   Boicu, Marius ^a   Huber, Robert ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CRYSTAL ORIENTATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DNA; ELECTRON TRANSPORT PROPERTIES; REDUCTION; RNA;

PATTERSON SEARCH TECHNIQUES;

BIOCHEMISTRY;

ADENINE; COMPLEMENTARY DNA; FERREDOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; IRON DERIVATIVE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PLANT RNA; PROTEIN PRECURSOR; RECOMBINANT PROTEIN; SULFUR DERIVATIVE; TYROSINE; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE REDUCTASE; FERREDOXIN-NAD+ REDUCTASE; OXIDOREDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; COMPLEX FORMATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; ELECTRON TRANSPORT; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE SEQUENCE; MOLECULAR CLONING; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PEPPER; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SPINACH; STRUCTURE ANALYSIS; TECHNIQUE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; MEDICINAL PLANT; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

CAPSICUM; CAPSICUM ANNUUM; ESCHERICHIA COLI; SPINACIA OLERACEA;

AMINO ACID SEQUENCE; CAPSICUM; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PLANTS, MEDICINAL; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0035937861     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M004576200     Document Type: Article

References (57)

1. Carrillo, N., and Vallejos, R. H. (1987) Topics Photosynth. 8, 527-560
2. Arakaki, A. K., Ceccarelli, E. A., and Carrillo, N. (1997) FASEB J. 11, 133-140
3. Karplus, P. A., Daniels, M. J., and Herriott, J. R. (1991) Science 251, 60-66
4. Bruns, C. M., and Karplus, P. A. (1995) J. Mol. Biol. 247, 125-145
5. Serre, L., Vellieux, M. D., Medina, M., Gómez-Moreno, C., Fontecilla-Camps, J. C., and Frey, M. (1996) J. Mol. Biol. 263, 20-39
6. Deng, Z., Aliverti, A., Zanetti, G., Arakaki, A. K., Ottado, J., Orellano, E. G., Calcaterra, N. B., Ceccarelli, E. A., Carrillo, N., and Karplus, P. A. (1999) Nat. Struct. Biol. 6, 847-853
7. Correll, C. C., Ludwig, M. L., Bruns, C. M., and Karplus, P. A. (1993) Protein Sci. 2, 2112-2133
8. Correll, C. C., Batie, C. J., Ballou, D. P., and Ludwig, M. L. (1992) Science 258, 1604-1610
9. Lu, G., Campbell, W. H., Schneider, G., and Lindqvist, Y. (1994) Structure 2, 809-821
10. Nishida, H., Inaka, K., Yamanaka, M., Kaida, S., Kobayashi, K., and Miki, K. (1995) Biochemistry 34, 2763-2767
11. Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S. S., and Kim, J. J. P. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 8411-8416
12. Ingelman, M., Bianchi, V., and Eklund, H. (1997) J. Mol. Biol. 268, 147-157
13. Foust, G. P., Mayhew, S. G., and Massey, V. (1969) J. Biol. Chem. 244, 964-979
14. De Pascalis, A. R., Jelesarow, I., Ackermann, F., Koppenol, W. H., Hirasawa, M., Knaff, D. B., and Bosshard H. R. (1993) Protein Sci. 2, 1126-1135
15. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
16. Aliverti, A., Jansen, T., Zanetti, G., Ronchi, S., Herrmann, R. G., and Curti, B. (1990) Eur. J. Biochem. 191, 551-555
17. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254
18. Leslie, A. G. W. (1991) Recent Changes to the MOSFLM Package for Processing Film and Image Plate Data, SERC Laboratory, Daresbury, Warrington, UK
19. Collaborative Computational Project 4 (1994) Acta Crystallogr. Sec. D 50, 760-763
20. Navaza, J. (1994) Acta Crystallogr. Sec. A 50, 157-163
21. Tong, L. A., and Rossmann, M. G. (1990) Acta Crystallogr. Sec. A 46, 783-792
22. Brünger, A. T. (1992) X-PLOR, a System for Crystallography and NMR, version 3.1, Yale University Press, New Haven, CT
23. Engh, R. A., and Huber, R. (1991) Acta Crystallogr. Sec. A 47, 392-400
24. Jones, T. A. (1985) Methods Enzymol. 115, 157-171
25. Turk, D. (1992) Weiterentwicklung eines Programms für Molekülgrahik und Elektronendichte-Manipulation und seine Anwendung auf verschiedene Protein-Strukturaufklärungen, Ph.D. thesis, Technical University Munich
26. Kleywegt, G. J., and Jones, T. A. (1994) ESF/CCP 4 Newsletter 31, 9-14
27. Kleywegt, G. J., and Jones, T. A. (1998) Acta Crystallogr. Sec. D 54, 1119-1131
28. Brünger, A. T. (1992) Nature 355, 472-474
29. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
30. Katchalski-Katzir, E., Shariv, I., Eisenstein, M., Friesem, A. A., Aflalo, C., and Vakser, I. A. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 2195-2199
31. Gabb, H. A., Jackson, R. M., and Sternberg, M. J. E. (1997) J. Mol. Biol. 272, 106-120
32. Binda, C., Coda, A., Aliverti, A., Zanetti, G., and Mattevi, A. (1998) Acta Crystallogr. Sec. D 54, 1353-1358
33. Jackson, R. M., Gabb, H. A., and Sternberg, M. J. E. (1998) J. Mol. Biol. 276, 265-285
34. Jones, T. A., and Kjelgaard, M. (1991) O: The Manual, University of Uppsala, Uppsala, Sweden
35. 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. Sec. D 54, 905-921
36. Barton, G. J. (1993) Protein Eng. 6, 37-40
37. Luzzatti, V. (1952) Acta Crystallogr. Sec. A 5, 802-810
38. Read, R. J. (1986) Acta Crystallogr. Sec. A 42, 140-149
39. Ramachandran, G. N., and Sasisekharan, V. (1968) Adv. Protein Chem. 23, 283-437
40. Kraulis, J. (1991) J. Appl. Crystallogr. 24, 946-950
41. Merritt, E. A., and Bacon, D. J. (1997) Methods Enzymol. 277, 505-524
42. Rossmann, M. G., Liljas, A., Brändén, C.-I., and Banaszak, L. J. (1975) The Enzymes 11, 61-102
43. Evans, S. V. (1993) J. Mol. Graphics 11, 134-138
44. Knaff, D. B., and Hirasawa, M. (1991) Biochim. Biophys. Acta 1056, 93-125
45. Jelesarow, W., DePascalis, A. R., Koppenol, W. H., Hirasawa, M., Knaff, D. B., and Bosshard, H. R. (1993) Eur. J. Biochem. 216, 57-66
46. Medina, M., Méndez, E., and Gómez-Moreno, C. (1992) FEBS Lett. 298, 25-28
47. Medina, M., Méndez, E., and Gómez-Moreno, C. (1992) Arch. Biochem. Biophys. 299, 281-286
48. Zanetti, G. Aliverti, A., and Curti, B. (1984) J. Biol. Chem. 259, 6153-6157
49. Zanetti, G., Morelli, D., Ronchi, S., Negri, A., Aliverti, A., and Curti, B. (1988) Biochemistry 27, 3753-3759
50. Hurley, J. K., Hazzard, J. T., Martinez-Júlvez, M., Medina, M., Gómez-Moreno, C., and Tollin, G. (1999) Protein Sci. 8, 1614-1622
51. Aliverti, A., Corrado, M. E., and Zanetti, J. (1994) FEBS Lett. 343, 247-250
52. Schmitz, S., Martinez-Júlvez, M., Gómez-Moreno, C., and Böhme, H. (1998) Biochim. Biophys. Acta 1363, 85-93
53. Karplus, P. A., and Bruns, C. M. (1994) J. Bioenerg. Biomembr. 26, 89-99
54. Marcus, R. A., and Sutin, N. (1985) Biochim. Biophys. Acta 811, 265-322
55. Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. (1984) J. Mol. Biol. 180, 385-398
56. Plato, M., Michel-Beyerle, M. E., Bixon, M., and Jortner, J. (1989) FEBS Lett. 249, 70-74
57. Chen, L., Durley, R. C. E., Mathews, F. S., and Davidson, V. L. (1994) Science 264, 86-90