Structure of Methanocaldococcus jannaschii nucleoside kinase: An archaeal member of the ribokinase family

Acta Crystallographica Section D: Biological Crystallography

Volumn 62, Issue 9, 2006, Pages 1085-1097

  Arnfors, Linda ^a   Hansen, Thomas ^b   Schönheit, Peter ^b   Ladenstein, Rudolf ^a   Meining, Winfried ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b UNIVERSITY OF KIEL   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOSIDE PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE; RECOMBINANT PROTEIN; RIBOKINASE;

AMINO ACID SEQUENCE; ARCHAEBACTERIUM; ARTICLE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; DIFFERENTIAL SCANNING CALORIMETRY; ELECTRON; ENZYMOLOGY; ESCHERICHIA COLI; METHANOCOCCUS; MOLECULAR GENETICS; MOLECULAR WEIGHT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ARCHAEA; CALORIMETRY, DIFFERENTIAL SCANNING; CRYSTALLIZATION; ELECTRONS; ESCHERICHIA COLI; METHANOCOCCUS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHOSPHOTRANSFERASES; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

ARCHAEA; ESCHERICHIA COLI; METHANOCALDOCOCCUS JANNASCHII; THERMOTOGA MARITIMA;

EID: 33748342136     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444906024826     Document Type: Article

References (48)

1. Andersson, C. E. & Mowbray, S. L. (2002). J. Mol. Biol. 315, 409-419.
2. Andreeva, A., Howorth, D., Brenner, S. E., Hubbard, T. J., Chothia, C. & Murzin, A. G. (2004). Nucleic Acids Res. 32, D226-D229.
3. Arnfors, L., Hansen, T., Meining, W., Schönheit, P. & Ladenstein, R. (2005). Acta Cryst. F61, 591-594.
4. Barton, G. J. (1993). Protein Eng. 6, 37-40.
5. Bork, P., Sander, C. & Valencia, A. (1993). Protein Sci. 2, 31-40.
6. 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. & Warren, G. L. (1998). Acta Cryst. D54, 905-921.
7. Burley, S. K. & Petsko, G. A. (1985). Science, 229, 23-28.
8. Campobasso, N., Mathews, I. I., Begley, T. P. & Ealick, S. E. (2000). Biochemistry, 39, 7868-7877.
9. Cheng, G., Bennett, E. M., Begley, T. P. & Ealick, S. E. (2002). Structure, 10, 225-235.
10. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
11. DeLano, W. L. (2002). The PyMOL Molecular Visualization System. http://www.pymol.org.
12. Dougherty, D. A. (1996). Science, 271, 163-168.
13. Hansen, T., Arnfors, L., Ladenstein, R. & Schönheit, P. (2006). In the press.
14. Holm, L. & Sander, C. (1993). J. Mol. Biol. 233, 123-138.
15. Ito, S., Fushinobu, S., Jeong, J. J., Yoshioka, I., Koga, S., Shoun, H. & Wakagi, T. (2003). J. Mol. Biol. 331, 871-883.
16. Ito, S., Fushinobu, S., Yoshioka, I., Koga, S., Matsuzawa, H. & Wakagi, T. (2001). Structure, 9, 205-214.
17. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
18. Kabsch, W. & Sander, C. (1983). Biopolymers, 22, 2577-2637.
19. Karshikoff, A. & Ladenstein, R. (2001). Trends Biochem. Sci. 26, 550-556.
20. Kleywegt, G. J. & Jones, T. A. (1994). Jnt CCP4/ESF-EACBM Newsl. Protein Crystallogr. 31, 9-14.
21. Lamzin, V. S. (1993). Acta Cryst. D49, 129-147.
22. Laskowski, R. A., Moss, D. S. & Thornton, J. M. (1993). J. Mol. Biol. 231, 1049-1067.
23. Li, M. H., Kwok, F., Chang, W. R., Lau, C. K., Zhang, J. P., Lo, S. C., Jiang, T. & Liang, D.-C. (2002). J. Biol. Chem. 277, 46385-46390.
24. McDonald, I. K. & Thornton, J. M. (1994). J. Mol. Biol. 238, 777-793.
25. Mathews, I. I., Erion, M. D. & Ealick, S. E. (1998). Biochemistry, 37, 15607-15620.
26. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
27. Murshudov, G. N. (1997). Acta Cryst. D53, 240-255.
28. Murzin, A. G., Brenner, S. E., Hubbard, T. & Chothia, C. (1995). J. Mol. Biol. 247, 536-540.
29. Ohshima, N., Inagaki, E., Yasuike, K., Takio, K. & Tahirov, T. H. (2004). J. Mol. Biol. 340, 477-489.
30. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
31. Perrakis, A. (1997). Acta Cryst. D53, 448-455.
32. Read, R. J. & Schierbeek, A. J. (1988). J. Appl. Cryst. 21, 490-495.
33. Russell, R. B. & Barton, G. J. (1992). Proteins, 14, 309-323.
34. Safo, M. K., Musayev, F. N., Hunt, S., di Salvo, M. L., Scarsdale, N. & Schirch, V. (2004). J. Bacteriol. 186, 8074-8082.
35. Schumacher, M. A., Scott, D. M., Mathews, I. I., Ealick, S. E., Roos, D. S., Ullman, B. & Brennan, R. G. (2000). J. Mol. Biol. 298, 875-893.
36. Sigrell, J. A., Cameron, A. D., Jones, T. A. & Mowbray, S. L. (1998). Structure, 6, 183-193.
37. Sigrell, J. A., Cameron, A. D. & Mowbray, S. L. (1999). J. Mol. Biol. 290, 1009-1018.
38. Spassov, V. Z., Karshikoff, A. D. & Ladenstein, R. (1995). Protein Sci. 4, 1516-1527.
39. Terwilliger, T. C. (2003). Acta Cryst. D59, 38-44.
40. Terwilliger, T. C. (2000). Acta Cryst. D56, 965-972.
41. Terwilliger, T. C. & Berendzen, J. (1999). Acta Cryst. D55, 849-861.
42. Tsuge, H., Sakuraba, H., Kobe, T., Kujime, A., Katunuma, N. & Ohshima, T. (2002). Protein Sci. 11, 2456-2463.
43. Vaguine, A. A., Richelle, J. & Wodak, S. J. (1999). Acta Cryst. D55, 191-205.
44. Wu, L.-F., Reizer, A., Reizer, J., Cai, B., Tomich, J. M. & Saier, M.H. Jr (1991). J. Bacteriol. 173, 3117-3127.
45. Yip, K. S., Artymiuk, P. J., Baker, P. J., Sedelnikova, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R. & Consalvi, V. (1995). Structure, 3, 1147-1158.
46. Yip, K. S., Britton, K. L., Stillman, T. J., Lebbink, J., de Vos, W. M., Robb, F. T., Vetriani, C., Maeder, D. & Rice, D. W. (1998). Eur. J. Biochem. 255, 336-346.
47. Zhang, R. G., Grembecka, J., Vinokour, E., Collart, F., Dementieva, I., Minor, W. & Joachimiak, A. (2002). J. Struct. Biol. 139, 161-170.
48. Zhang, Y., Dougherty, M., Downs, D. M. & Ealick, S. E. (2004). Structure, 12, 1809-1821.