Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution

Science

Volumn 275, Issue 5307, 1997, Pages 1800-1804

  Park, Hee Won ^a   Boduluri, Sobha R ^a   Moomaw, John F ^a   Casey, Patrick J ^a   Beese, Lorena S ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN FARNESYLTRANSFERASE; ZINC;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN;

ALKYL AND ARYL TRANSFERASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SEQUENCE ALIGNMENT; TRANSFERASES; ZINC;

ANIMALIA; MAMMALIA;

EID: 0030909826     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5307.1800     Document Type: Article

References (62)

1. F. L. Zhang and P. J. Casey, Annu. Rev. Biochem. 65, 241 (1996); W. R. Schafer and J. Rine, Annu. Rev. Genetics 25, 209 (1992); J. A. Glomset and C. C. Farnsworth, Annu. Rev. Cell. Biol. 10, 181 (1994).
2. F. L. Zhang and P. J. Casey, Annu. Rev. Biochem. 65, 241 (1996); W. R. Schafer and J. Rine, Annu. Rev. Genetics 25, 209 (1992); J. A. Glomset and C. C. Farnsworth, Annu. Rev. Cell. Biol. 10, 181 (1994).
3. F. L. Zhang and P. J. Casey, Annu. Rev. Biochem. 65, 241 (1996); W. R. Schafer and J. Rine, Annu. Rev. Genetics 25, 209 (1992); J. A. Glomset and C. C. Farnsworth, Annu. Rev. Cell. Biol. 10, 181 (1994).
4. W. R. Schafer et al., Science 245, 379 (1989).
5. P. J. Casey, P. A. Solski, C. J. Der, J. E. Buss, Proc. Natl. Acad. Sci. U.S.A. 86, 8323 (1989).
6. J. F. Hancock, A. I. Magee, J. E. Childs, C. J. Marshall, Cell 57, 1167 (1989).
7. G. L. James et al., Science 260, 1937 (1993); N. E. Kohl et al., ibid., p. 1934; J. B. Gibbs, A. Oliff, N. E. Kohl, Cell 77, 175 (1994); J. E. Buss and J. C. Marsters, Chem. Biol. 2, 787 (1995).
8. G. L. James et al., Science 260, 1937 (1993); N. E. Kohl et al., ibid., p. 1934; J. B. Gibbs, A. Oliff, N. E. Kohl, Cell 77, 175 (1994); J. E. Buss and J. C. Marsters, Chem. Biol. 2, 787 (1995).
9. G. L. James et al., Science 260, 1937 (1993); N. E. Kohl et al., ibid., p. 1934; J. B. Gibbs, A. Oliff, N. E. Kohl, Cell 77, 175 (1994); J. E. Buss and J. C. Marsters, Chem. Biol. 2, 787 (1995).
10. G. L. James et al., Science 260, 1937 (1993); N. E. Kohl et al., ibid., p. 1934; J. B. Gibbs, A. Oliff, N. E. Kohl, Cell 77, 175 (1994); J. E. Buss and J. C. Marsters, Chem. Biol. 2, 787 (1995).
11. N. E. Kohl et al., Nature Med. 1, 792 (1995).
12. Y. Reiss, J. L. Goldstein, M. C. Seabra, P. J. Casey, M. S. Brown, Cell 162, 81 (1990); W.-J. Chen, D. A. Andres, J. L. Goldstein, D. W. Russell, M. S. Brown, ibid. 66, 327 (1991); W.-J. Chen, D. A. Andres, J. L. Goldstein, M. S. Brown, Proc. Natl. Acad. Sci. U.S.A. 88, 11368 (1991).
13. Y. Reiss, J. L. Goldstein, M. C. Seabra, P. J. Casey, M. S. Brown, Cell 162, 81 (1990); W.-J. Chen, D. A. Andres, J. L. Goldstein, D. W. Russell, M. S. Brown, ibid. 66, 327 (1991); W.-J. Chen, D. A. Andres, J. L. Goldstein, M. S. Brown, Proc. Natl. Acad. Sci. U.S.A. 88, 11368 (1991).
14. Y. Reiss, J. L. Goldstein, M. C. Seabra, P. J. Casey, M. S. Brown, Cell 162, 81 (1990); W.-J. Chen, D. A. Andres, J. L. Goldstein, D. W. Russell, M. S. Brown, ibid. 66, 327 (1991); W.-J. Chen, D. A. Andres, J. L. Goldstein, M. S. Brown, Proc. Natl. Acad. Sci. U.S.A. 88, 11368 (1991).
15. M. C. Seabra, Y. Reiss, P. J. Casey, M. S. Brown, J. L. Goldstein, Cell 65, 429 (1991); F. L. Zhang et al., J. Biol. Chem. 269, 3175 (1994).
16. M. C. Seabra, Y. Reiss, P. J. Casey, M. S. Brown, J. L. Goldstein, Cell 65, 429 (1991); F. L. Zhang et al., J. Biol. Chem. 269, 3175 (1994).
17. S. L. Moores et al., J. Biol. Chem. 266, 14603 (1991).
18. Y. Reiss, M. S. Brown, J. L. Goldstein, ibid. 267, 6403 (1992); F. L. Zhang, J. F. Moomaw, P. J. Casey, ibid. 269, 23465 (1994); J. F. Moomaw and P. J. Casey, ibid. 267, 17438 (1992); P. J. Casey and M. C. Seabra, ibid. 271, 5289 (1996).
19. Y. Reiss, M. S. Brown, J. L. Goldstein, ibid. 267, 6403 (1992); F. L. Zhang, J. F. Moomaw, P. J. Casey, ibid. 269, 23465 (1994); J. F. Moomaw and P. J. Casey, ibid. 267, 17438 (1992); P. J. Casey and M. C. Seabra, ibid. 271, 5289 (1996).
20. Y. Reiss, M. S. Brown, J. L. Goldstein, ibid. 267, 6403 (1992); F. L. Zhang, J. F. Moomaw, P. J. Casey, ibid. 269, 23465 (1994); J. F. Moomaw and P. J. Casey, ibid. 267, 17438 (1992); P. J. Casey and M. C. Seabra, ibid. 271, 5289 (1996).
21. Y. Reiss, M. S. Brown, J. L. Goldstein, ibid. 267, 6403 (1992); F. L. Zhang, J. F. Moomaw, P. J. Casey, ibid. 269, 23465 (1994); J. F. Moomaw and P. J. Casey, ibid. 267, 17438 (1992); P. J. Casey and M. C. Seabra, ibid. 271, 5289 (1996).
22. C.-C. Huang, P. J. Casey, C. A. Fierke, ibid. 272, 20 (1997).
23. W.-J. Chen, J. F. Moomaw, L. Overton, T. A. Kost, P. J. Casey, ibid. 268, 9675 (1993).
24. 5 with unit cell dimensions A = B = 167.06 Å, and C = 97.90 Å. There is one FTase heterodimer in the asymmetric unit.
25. K. Cowtan, Newsl. Protein Crystallogr. 31, 34 (1994).
26. R. J. Read, Acta Crystallogr. A42, 140 (1986).
27. A. T. Brunger, X-PLOR version 3.1. A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, CT, 1992).
28. A. M. Thunnissen et al., Nature 367, 750 (1994).
29. R. Raag, K. Appelt, N. H. Xuong, L. Banaszak, J. Mol. Biol. 200, 553 (1988).
30. P. M. Alzari, H. Souchon, R. Dominguez, Structure 4, 265 (1996); A. Aleshin, A. Golubev, L. M. Firsov, R. B. Honzatko, J. Biol. Chem. 267, 19291 (1992); A. E. Aleshin, C. Hoffman, L. M. Firsov, R. B. Honzatko, J. Mol. Biol. 238, 575 (1994); M. Juy et al., Nature 357, 89 (1992).
31. P. M. Alzari, H. Souchon, R. Dominguez, Structure 4, 265 (1996); A. Aleshin, A. Golubev, L. M. Firsov, R. B. Honzatko, J. Biol. Chem. 267, 19291 (1992); A. E. Aleshin, C. Hoffman, L. M. Firsov, R. B. Honzatko, J. Mol. Biol. 238, 575 (1994); M. Juy et al., Nature 357, 89 (1992).
32. P. M. Alzari, H. Souchon, R. Dominguez, Structure 4, 265 (1996); A. Aleshin, A. Golubev, L. M. Firsov, R. B. Honzatko, J. Biol. Chem. 267, 19291 (1992); A. E. Aleshin, C. Hoffman, L. M. Firsov, R. B. Honzatko, J. Mol. Biol. 238, 575 (1994); M. Juy et al., Nature 357, 89 (1992).
33. P. M. Alzari, H. Souchon, R. Dominguez, Structure 4, 265 (1996); A. Aleshin, A. Golubev, L. M. Firsov, R. B. Honzatko, J. Biol. Chem. 267, 19291 (1992); A. E. Aleshin, C. Hoffman, L. M. Firsov, R. B. Honzatko, J. Mol. Biol. 238, 575 (1994); M. Juy et al., Nature 357, 89 (1992).
34. M. Boguski, A. W. Murray, S. Powers, New Biol. 4, 408 (1992).
35. Collaborative Computational Project No 4., Acta. Crystallogr. D50, 760 (1994).
36. J. Jainin, S. Miller, C. Chothia, J. Mol. Biol. 204, 155 (1988).
37. C. A. Omer et al., Biochemistry 32, 5167 (1993).
38. H. W. Fu, J. F. Moomaw, C. R. Moomaw, P. J. Casey, J. Biol. Chem. 271, 28541 (1996).
39. B. L. Vallee and D. S. Auld, Biochemistry 29, 5647 (1990); D. W. Cristianson, Adv. Protein Chem. 42, 281 (1991).
40. B. L. Vallee and D. S. Auld, Biochemistry 29, 5647 (1990); D. W. Cristianson, Adv. Protein Chem. 42, 281 (1991).
41. Y. Reiss et al., J. Biol. Chem. 266, 10672 (1991); Y. E. Bukhtiyarov, C. A. Omer, C. M. Allen, ibid. 270, 19035 (1995); K. Yokoyama, P. McGeady, M. H. Gelb, Biochemistry 34, 1344 (1995).
42. Y. Reiss et al., J. Biol. Chem. 266, 10672 (1991); Y. E. Bukhtiyarov, C. A. Omer, C. M. Allen, ibid. 270, 19035 (1995); K. Yokoyama, P. McGeady, M. H. Gelb, Biochemistry 34, 1344 (1995).
43. Y. Reiss et al., J. Biol. Chem. 266, 10672 (1991); Y. E. Bukhtiyarov, C. A. Omer, C. M. Allen, ibid. 270, 19035 (1995); K. Yokoyama, P. McGeady, M. H. Gelb, Biochemistry 34, 1344 (1995).
44. W. Ying, L. Sepp-Lorenzino, K. Cai, P. Aloise, P. S. Coleman, J. Biol. Chem. 269, 470 (1994).
45. The distances were measured between the peptide backbones of opposite helices in the core.
46. E. S. Furfine, J. J. Leban, A. Landavazo, J. F. Moomaw, P. J. Casey, Biochemistry 34, 6857 (1995).
47. L. C. Tarshis, M. Yan, C. D. Poulter, J. C. Sacchettini, ibid. 33, 10871 (1994).
48. K. Padmenabhan et al., J. Mol. Biol. 232, 947 (1993).
49. The phi psi angles for an ideal type I β turn are-60°, -30°, -90°, and 0°. In the nonapeptide we observed these angles to be -44°, -24°, -83°, and 8°. The distortion from ideality may arise from the proline in the fourth position.
50. S. J. Stradely, J. Rizo, L. Gierasch, Biochemistry 32, 12586 (1993).
51. D. A. Andres et al., J. Biol. Chem. 268, 1383 (1993).
52. G. L. James, J. L. Goldstein, M. S. Brown, ibid. 270, 6221 (1995).
53. Z. Otwinowski, in Proceedings of the CCP4 Study Weekend, L. Sawyer, N. Isaac, S. Borley, Eds. (SERC Daresbury, Daresbury, UK, 1993), pp. 56-62.
54. S. Knight, thesis, Swedish University of Agricultural Sciences, Uppsala, 1989.
55. Z. Otwinowski, in Isomorphous Replacement and Anomalous Scattering, W. Wolf, P. R. Evans, A. G. W. Leslie, Eds. (Science and Engineering Research Council, Warrington, UK, 1991), p. 80.
56. T. A. Jones and M. Kjeldgaard, O version 5.9. The Manual (Uppsala University, Uppsala, Sweden, 1993).
57. P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991).
58. E. A. Merritt and M. E. P. Murphy, Acta. Crystallogr. D50, 869 (1994).
59. R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993).
60. INSIGHT II: User Guide (Biosym Technologies, San Diego, CA, 1993).
61. A. Nicholls, GRASP: Graphical Representation and Analysis of Surface Properties (Columbia University, New York, 1992).
62. Supported by NIH grant GM52382, Searle Scholar Foundation, and Schering-Plough Research Institute to L.S.B., and by NIH grant GM46372 and Council for Tobacco Research grant 4064 to P.J.C. We thank G. Petsko for ethyl mercury phosphate, A. Mondragon for advice on freezing FTase crystals, J. Richardson for advice on structural homology, and H. W. Hellinga for discussions and editorial assistance. We also thank the Keck Foundation for support of the Levine Science Research Center at Duke University. The coordinates have been deposited with the Brookhaven Protein Data Bank.