Structure of Yeast Triosephosphate Isomerase at 1.9-Å Resolution

Biochemistry

Volumn 29, Issue 28, 1990, Pages 6609-6618

  Lolis, Elias ^a   Alber, Tom ^b   Davenport, Robert C ^a   Rose, David ^c   Hartman, Fred C ^d   Petsko, Gregory A ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^c NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^d OAK RIDGE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; ENZYME STRUCTURE; FUNGUS; NONHUMAN; PRIORITY JOURNAL; X RAY ANALYSIS; YEAST;

AMINO ACID SEQUENCE; BINDING SITES; CARBOHYDRATE EPIMERASES; COMPARATIVE STUDY; EVOLUTION; FUNGAL PROTEINS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, NUCLEIC ACID; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; TRIOSE-PHOSPHATE ISOMERASE; X-RAY DIFFRACTION;

ESCHERICHIA COLI; FUNGI;

EID: 0025358007     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00480a009     Document Type: Article

References (75)

1. Ahern, T. J., Casal, J. I., Petsko, G. A., & Klibanov, A. M. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 675–679.
2. Alber, T., & Kawasaki, G. (1982) J. Mol. Appl. Genet. 1, 419–434.
3. Alber, T., Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Rivers, P. S., & Wilson, I. A. (1981a) Philos. Trans. R. Soc. London, B 293, 159–171.
4. Alber, T., Hartman, F. C., Johnson, R. M., Petsko, G. A., & Tsernoglou, D. (1981b) J. Biol. Chem. 256, 1356–1361.
5. Alber, T. C., Davenport, R. C., Giammona, D. A., Lolis, E., Petsko, G. A., & Ringe, D. (1987) Cold Spring Harbor Sy mp. Quant. Biol. 52, 603–613.
6. Albery, W. J., & Knowles, J. R. (1976) Biochemistry 15, 5627–5640.
7. Albery, W. J., & Knowles, J. R. (1977) Angew. Chem., Int. Ed. Engl. 16, 285–293.
8. Arnone, A., Bier, C. J., Cotton, F. A., Day, V. W., Hazen, E. E., Richardson, D. C., Richardson, J. S., & Yonath, A. (1971) J. Biol. Chem. 246, 2302.
9. Artavanis-Tsakonis, S., & Harris, J. J. (1980) Eur. J. Bio chem. 108, 599–611.
10. Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Pogson, C. I., & Wilson, I. A. (1975) Nature 255, 609.
11. Belasco, J. G., Herlihy, J. M., & Knowles, J. R. (1978) Biochemistry 17, 2971–2978.
12. Blacklow, S. C., Raines, R. T., Lim, W. A., Zamore, P. D., & Knowles, J. R. (1988) Biochemistry 27, 1158–1167.
13. Blow, D. M., & Crick, F. H. C. (1959) Acta Crystallogr. 12, 794–803.
14. Brunger, A. T., Kuriyan, J., & Karplus, M. (1987) Science 235, 458–460.
15. Buisson, G., Duce, E., Haser, R., & Payan, F. (1987) EMBO J. 6, 3909–3916.
16. Campbell, R. L. (1988) Ph.D. Thesis, Massachusetts Institute of Technology.
17. Casal, J. I., Ahern, T. J., Davenport, R. C., Petsko, G. A., & Klibanov, A. M. (1987) Biochemistry 26, 1258–1264.
18. Chambers, J. L., & Stroud, R. M. (1979) Acta Crystallogr. 35, 1861–1874.
19. Chapman, M. S., Suh, S. W., Curmi, P. M. G., Cascio, D., Smith, W. W., & Eisenberg, D. S. (1988) Science 241, 71–74.
20. Chou, P. Y., & Fasman, G. D. (1977) J. Mol. Biol. 115, 135–175.
21. Corran, P. H., & Waley, S. G. (1975) Biochem. J. 137, 335–344.
22. Daar, I. O., Artymiuk, P. J., Phillips, D. C., & Maqaut, L. E. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7903–7907.
23. De la Mare, S., Coulson, A. F. W., Knowles, J. R., Priddel, J. D., & Offord, R. E. (1972) Biochem. J. 129, 321–331.
24. Dodson, E. J., & Vijayan, M. (1971) Acta Crystallogr. 27, 2402–2411.
25. Färber, G. K., Petsko, G. A., & Ringe, D. (1987) Protein Eng. 1, 459–466.
26. Fraser, R. D. B., McRae, T. P., & Suzuki, E. (1978) J. Appl. Crystallogr. 11, 693–694.
27. Goldman, A., Ollis, D. L., & Steitz, T. A. (1987) J. Mol. Biol. 194, 143–153.
28. Hartman, F. C. (1971) Biochemistry 10, 146–154.
29. Hendrickson, W. A. (1985) in Methods in Enzymology Wyckoff, H. W., Hirs, C. H. W., & Timasheff, S. N., Eds.) Vol. 115, pp 252–270, Academic Press, New York.
30. Henrick, K., Blow, D. M., Carrell, H. L., & Glusker, J. P. (1987) Protein Eng. 1, 461–469.
31. Hill, E., Tsernoglou, D., Webb, L., & Banazak, L. J. (1972) J. Mol. Biol. 72, 577–591.
32. Hol, W. J. G., Van Duijnen, P. T., & Berendsen, H. J. (1978) Nature 273, 443.
33. Hyde, C. C., Padlan, E. A., Ahmed, S. A., Miles, E. W., & Davie, D. R. (1987) Fed. Proc., Fed. Am. Soc. Exp. Biol. 46, 2215.
34. Jones, T. A., & Thirup, S. (1986) EMBO J. 5, 819–822.
35. Knowles, J. R., & Albery, W. J. (1977) Acc. Chem. Res. 10, 105–111.
36. Kolb, E., Harris, J. J., & Bridger, J. (1974) Biochem. J. 137, 185–197.
37. Lasters, I., Wodak, S. J., Alard, P., & Van Cutsem, E. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 3338–3342.
38. Lebioda, L., & Stec, B. (1988) Nature 333, 683–686.
39. Lim, L. W., Shamala, N., Mathews, F. S., Steenkamp, D. J., Hamlin, R., & Xuong, N. H. (1986) J. Biol. Chem. 261, 15140–15146.
40. Lindqvist, Y., & Branden, C.-I. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 6855–6859.
41. Lolis, E., & Petsko, G. A. (1990) Biochemistry (following paper in this issue).
42. Lu, H. S., Yuan, P. M., & Gracy, R. W. (1984) J. Biol. Chem. 259, 11958–11968.
43. Luzzati, V. (1952) Acta Crystallogr. 5, 802–810.
44. Maquat, L. E., Chilote, R., & Ryan, P. M. (1985) J. Biol. Chem. 260, 3748–3753.
45. Marchionni, M., & Gilbert, W. (1986) Cell 46, 133–141.
46. Matsuua, Y., Kusunoki, M., Harada, W., & Kakudo, M. (1984) J. Biochem. 95, 697–702.
47. Matthews, B. W. (1966a) Acta Crystallogr. 20, 82–86.
48. Matthews, B. W. (1966b) Acta Crystallogr. 20, 230–239.
49. Matthews, B. W., & Czerwinski, G. W. (1975) Acta Crystallogr. 31, 480–487.
50. Mavridis, J. M., Hatada, M. H., Tulinskky, A., & Lebioda, L. (1982) J. Mol. Biol. 162, 419–444.
51. McKnight, G. L., O’Hara, P. J., & Parker, M. L. (1986) Cell 46, 143–147.
52. Miller J. C., & Waley, S. G. (1971) Biochem. J. 123, 163–170.
53. Nickbarg, E. B., & Knowles, J. R. (1988) Biochemistry 27, 5939–5947.
54. Nickbarg, E. B., Davenport, R. C., Petsko, G. A., & Knowles, J. R. (1988) Biochemistry 27, 5948–5960.
55. North, A. C. T., Phillips, D. C., & Mathew, F. S. (1968) Acta Crystallogr. 24, 351–359.
56. Old, S. E., & Mohrenweiser, H. W. (1988) Nucleic Acids Res. 16, 9055.
57. Phillips, D. C., Sternberg, M. J. E., Thornton, J. M., & Wilson, I. A. (1977) Biochem. Soc. Trans. 72,642–647.
58. Pichersky, E., Gottlieb, L. D., & Hess, J. P. (1984) Mol. Gen. Genet. 195, 314–320.
59. Priestie, J. P., Grutter, M. G., White, J. L., Vincent, M. G., Kania, M., Wilson, E., Jardetzky, T. S., Kirschner, K., & Jansonius, J. N. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 5690–5694.
60. Rao, S. T., Hogle, J., & Sundaralingam, M. (1983) Acta Crystallogr. 39, 237–240.
61. Richard, J. P. (1984) J. Am. Chem. Soc. 106, 4926.
62. Richards, F. M. (1977) Annu. Rev. Biophys. Bioeng. 6, 151–176.
63. Russell, P. R. (1985) Gene 40, 125–130.
64. Sali, D., Bycroft, M., & Fersht, A. R. (1988) Nature 335, 740–743.
65. Schneider, G., Lindqvist, Y., Branden, C.-I., & Lorimer, G. (1986) EMBO J. 5, 3409–3415.
66. Straus, D., & Gilbert, W. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 2014–2018.
67. Straus, D., Raines, R., Kawashima, E., Knowles, J. R., & Gilbert, W. (1985) Proc. Natl. Acad. Soc. U.S.A. 82, 2272–2276.
68. Stuart, D. I., Levine, M., Muirhead, H., & Stammers, D. K. (1979) J. Mol. Biol. 134, 109–142.
69. Swinkles, B. W., Gibson, W. C., Osingas, K. A., Kramer, R., Veeneman, G. H., Van Boon, J. H., & Berst, P. (1986) EMBO J. 5, 1291–1298.
70. Sygusch, J., Beaudry, D., & Allaire, M. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 7846–7850.
71. Valentine, W. N., Tanaka, K. R., & Paglia, D. E. (1983) in The Metabolic Basis of Inherited Disease (Stanbury, J. B., Wyngaarden, J. B., Frederickson, D. S., Goldstein, J. L., & Brown, M. S., Eds.) pp 1606–1682, McGraw-Hill Book Co., New York.
72. Wierenga, R. K., Kalk, K. H., & Hol, W. J. G. (1987) J. Mol. Biol. 198, 109–121.
73. Wolfenden, R. (1969) Nature 223, 704.
74. Wyckoff, H. W., Doscher, M., Tsernoglou, D., Inagami, Y., Johnson, L. N., Hardman, K. D., Allewell, N. M., Kelly, D. M., & Richards, F. M. (1967) J. Mol. Biol. 27, 563–578.
75. Xia, Z.-X., Shamala, N., Bethge, P. H., Lim, L. W., Bellamy, H. D., Xuong, N. H., Lederer, F., & Mathews, F. S. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 2629–2633.