Crystal Structure of the Bifunctional Chorismate Synthase from Saccharomyces cerevisiae

Journal of Biological Chemistry

Volumn 279, Issue 1, 2004, Pages 619-625

  Quevillon Cheruel, Sophie ^a   Leulliot, Nicolas ^a   Meyer, Philippe ^a   Graille, Marc ^b   Bremang, Michael ^a   Blondeau, Karine ^c   Sorel, Isabelle ^b   Poupon, Anne ^b   Janin, Joël ^b   Van Tilbeurgh, Herman ^a,b  

^a INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

^b LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^c UNIVERSITÉ PARIS SACLAY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; BIOSYNTHESIS; CARRIER CONCENTRATION; CATALYSIS; CRYSTAL STRUCTURE; ENZYMES; FUNGI; PHOSPHORIC ACID; SPECTROSCOPY; X RAY ANALYSIS;

STRUCTURAL CHANGES;

BIOCHEMISTRY;

AMINO ACID; CHORISMATE SYNTHASE; FUNGAL ENZYME; SELENOMETHIONINE; TETRAMER; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CATALYSIS; CONTROLLED STUDY; CRYSTAL; CRYSTAL STRUCTURE; ELECTRON; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; HUMAN; MOLECULE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; X RAY ANALYSIS; YEAST;

AMINO ACID SEQUENCE; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHORUS-OXYGEN LYASES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SENSITIVITY AND SPECIFICITY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 9144259546     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M310380200     Document Type: Article

References (32)

1. Bentley, R. (1990) Crit. Rev. Biochem. Mol. Biol. 25, 307-384
2. Roberts, F., Roberts, C. W., Johnson, J. J., Kyle, D. E., Krell, T., Coggins, J. R., Coombs, G. H., Milhous, W. K., Tzipori, S., Ferguson, D. J., Chakrabarti, D., and McLeod, R. (1998) Nature 393, 801-805
3. White, P. J., Millar, G., and Coggins, J. R. (1988) Biochem. J. 251, 313-322
4. Macheroux, P., Schonbrunn, E., Svergun, D. I., Volkov, V. V., Koch, M. H., Bornemann, S., and Thorneley, R. N. (1998) Biochem. J. 335, 319-327
5. Hill, R. K., and Newkome, G. R. (1969) J. Am. Chem. Soc. 91, 5893-5894
6. Welch, G. R., Cole, K. W., and Gaertner, F. H. (1974) Arch. Biochem. Biophys. 165, 505-518
7. Bornemann, S., Lowe, D. J., and Thorneley, R. N. (1996) Biochemistry 35, 9907-9916
8. Henstrand, J. M., Schaller, A., Braun, M., Amrhein, N., and Schmid, J. (1996) Mol. Microbiol. 22, 859-866
9. Fitzpatrick, T., Ricken, S., Lanzer, M., Amrhein, N., Macheroux, P., and Kappes, B. (2001) Mol. Microbiol. 40, 65-75
10. Ahn, H. J., Yang, J. K., Lee, B. I., Yoon, H. J., Kim, H. W., and Suh, S. W. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 569-571
11. Hendrickson, W. A., Horton, J. R., and Lemaster, D. M. (1990) EMBO J. 9, 1665-1672
12. Van Duyne, P., Ray, M. V., Bertelsen, A. H., Jackson-Matthews, D. E., Sturmer, A. M., Merkler, D. J., Consalvo, A. P., Young, S. D., Gilligan, J. P., and Shields, P. P. (1993) Bio/Technology 11, 64-70
13. Collaborative Computational Project 4 (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
14. Terwilliger, T. C., and Berendzen, J. (1997) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 849-861
15. Perrakis, A., Morris, R. J., and Lamzin, V. S. (1999) Nat. Struct. Biol. 6, 458-463
16. Murshudov, G., Vagin, A., and Dodson, E. (1997) Acta Crystallogr. Sect. DBiol. Crystallogr. 53, 240-255
17. Jones, T. A., Zou, J. H., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sect. A 47, 110-119
18. Navaza, J. (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 53, 157-163
19. Lo Conte, L., Chothia, C., and Janin, J. (1999) J. Mol. Biol. 285, 2177-2198
20. Henstrand, J. M., Schmid, J., and Amrhein, N. (1995) Plant Physiol. 108, 1127-1132
21. Braun, M., Henstrand, J. M., Gorlach, J., Amrhein, N., and Schmid, J. (1996) Planta 200, 64-70
22. Macheroux, P., Petersen, J., Bornemann, S., Lowe, D. J., and Thorneley, R. N. (1996) Biochemistry 35, 1643-1652
23. Macheroux, P., Bornemann, S., Ghisla, S., and Thorneley, R. N. (1996) J. Biol. Chem. 271, 25850-25858
24. Henstrand, J. M., Amrhein, N., and Schmid, J. (1995) J. Biol. Chem. 270, 20447-20452
25. Baker, P. J., Britton, K. L., Rice, D. W., Rob, A., and Stillman, T. J. (1992) J. Mol. Biol. 228, 662-671
26. Carugo, O., and Argos, P. (1997) Proteins 28, 29-40
27. Wilson, D. K., Bohren, K. M., Gabbay, K. H., and Quiocho, F. A. (1992) Science 257, 81-84
28. Gouet, P., Jouve, H. M., and Dideberg, O. (1995) J. Mol. Biol. 249, 933-954
29. Mesecar, A. D., Stoddard, B. L., and Koshland, D. E., Jr. (1997) Science 277, 202-206
30. Xiong, J. P., Xia, Z. X., and Wang, Y. (1994) Nat. Struct. Biol. 1, 695-700
31. Gouet, P., Courcelle, E., Stuart, D. I., and Metoz, F. (1999) Bioinformatics 15, 305-308
32. Westhead, D. R., Hatton, D. C., and Thornton, J. M. (1998) Trends Biochem. Sci. 23, 35-36