Structure of the αβ tubulin dimer by electron crystallography

Nature

Volumn 391, Issue 6663, 1998, Pages 199-203

  Nogales, Eva ^a   Wolf, Sharon G ^a,b   Downing, Kenneth H ^a  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; TUBULIN;

ARTICLE; CRYSTAL STRUCTURE; DROSOPHILA; ELECTRON MICROSCOPY; MICROTUBULE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN DOMAIN; SWINE;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY; DIMERIZATION; ELECTRONS; GUANOSINE TRIPHOSPHATE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PACLITAXEL; PROTEIN CONFORMATION; SWINE; TUBULIN; ZINC;

EID: 0032495513     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/34465     Document Type: Article

References (30)

1. Ludveña, R. F. The multiple forms of tubulin: different gene products and covalent modifications. Int. Rev. Cyt. 178, 207-275 (1998).
2. Mukherjee, A. & Lutkenhaus, J. Guanine nucleotide-dependent assembly of FtsZ into filaments. J. Bacteriol. 176, 2754-2758 (1994).
3. Gabor Miklos, G. L., Yamamoto, M., Burns, R. G. & Maleszka, R. An essential cell division gene of Drosophila, absent from Saccharomyces, encodes an unusual protein with tubulin-like and myosin-like peptide motifs. Proc. Natl Acad. Sci. USA 94, 5189-5194 (1997).
4. Nogales, E., Wolf, S.G., Zhang, S. X. & Downing, K. H. Preservation of 2-D crystals of tubulin for electron crystallography. J. Struct. Biol. 115, 199-208 (1995).
5. Nogales, E., Wolf, S. G., Khan, I. A., Ludueña, R. F. & Downing, K. H. Structure of tubulin at 6.5 Å and location of the taxol-binding site. Nature 375, 424-427 (1995).
6. Nogales, E., Wolf, S. G. & Downing, K. H. Visualizing the secondary structure of tubulin: three-dimensional map at 4Å. J. Struct. Biol. 118, 119-127 (1997).
7. Burns, R. G. & Surridge, C. D. in Microtubules (eds Hyams, J. S. & Lloyd, C. W.) 3-32 (Wiley, New York, 1993).
8. Little, M. & Luduena, R. F. Structural differences between brain β1-and β2-tubulins: implications for microtubule assembly and colchicine binding. EMBO J. 4, 51-56 (1985).
9. Wolf, S. G., Nogales, E., Kikkawa, M., Gratzinger, D., Hirokawa, N. & Downing, K. H. Interpreting a medium-resolution model of tubulin: comparison of zinc-sheet and microtubule structure. J. Mol. Biol. 263, 485-501 (1996).
10. Shivanna, B. D., Mejillano, M. R., Williams, T. D. & Himes, R. H. Exchangeable GTP binding site of β-tubulin - identification of cysteine 12 as the major site of cross-linking by direct photoaffinity labeling. J. Biol. Chem. 268, 127-132 (1993).
11. Hesse, J., Thierauf, M. & Ponstingl, H. Tubulin sequence region β155-174 is involved in binding exchangeable guanosine triphosphate. J. Biol. Chem. 262, 15472-15475 (1987).
12. Linse, K. & Mandelkow, E.-M. The GTP-binding peptide of β-tubulin. Localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins. J. Biol. Chem. 263, 15205-15210 (1988).
13. Davis, A., Sage, C. R., Dougherty, C. A. & Farrell, K. W. Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of β-tubulin. Science 264, 839-842 (1994).
14. 1-tubulin that can be cross-linked after removal of exchangeable GTP. Biochim. Biophys. Acta 912, 28-33 (1987).
15. Bai, R. et al. Identification of cysteine 354 of β-tubulin as part of the binding site for the A ring of colchicine. J. Biol. Chem. 271, 12639-12645 (1996).
16. Uppuluri, S., Knipling, L., Sackett, D. L. & Wolff, J. Localization of the colchicine-binding site of tubulin. Proc. Natl Acad. Sci. USA 90, 11598-11602 (1993).
17. Shearwin, K. E. & Timasheff, S. N. Effect of colchicine analogs on the dissociation of αβ tubulin into subunits: the locus of colchicine binding. Biochemistry 33, 894-901 (1994).
18. Andreu, J. M. Site-directed antibodies to tubulin. Cell Motil. Cytoskel. 26, 1-6 (1993).
19. Caplow, M., Ruhlen, R. L. & Shanks, J. The free energy of hydrolysis of a microtubule-bound nucleoside triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice. J. Cell Biol. 127, 779-788 (1994).
20. Vale, R. D., Coppin, C. M., Malik, F., Kull, F. J. & Milligan, R. A. Tubulin GTP hydrolysis influences the structure, mechanical properties, and kinesin-driven transport of microtubules. J. Biol. Chem. 269, 23769-23775 (1994).
21. Hyman, A. A., Chrétien, D., Arnal, I. & Wade, R. H. Structural changes accompanying GTP hydrolysis of microtubules: information from a slowly hydrolyzable analog guanylyl-(γ,β)-methylene-diphosphonate. J. Cell Biol. 128, 117-125 (1995).
22. Diaz, J. F., Pantos, E., Bordas, J. & Andreu, J. M. Solution structure of GDP-tubulin double rings to 3 nm resolution and comparison with microtubules. J. Mol. Biol. 238, 214-225 (1994).
23. Mandelkow, E. & Mandelkow, E.-M. Microtubules and micro tubule-associated proteins. Curr. Opin. Cell Biol. 7, 72-81 (1995).
24. Gueritte-Voegelein, F. et al. Structure of a synthetic taxol precursor: N-tert-butoxycarbonyl-10-deacetyl-N-debenzoyltaxol. Acta Crystallogr. C 46, 781-784 (1990).
25. Rao, S., Krauss, N. E., Heerding, J. M., Orr, G. A. & Horwitz, S. B. 3′-(p-Azidobenzamido)taxol photolabels the N-terminal 31 amino acids of β-tubulin. J. Biol. Chem. 269, 3132-3134 (1994).
26. Rao, S., Orr, G. A., Chaudhary, A. G., Kingston, D. G. I. & Horwitz, S. B. Characterization of the taxol binding site on the microtubule. J. Biol. Chem. 270, 20235-20238 (1995).
27. Löwe, I. Y. & Amos, L. A. Crystal structure of the bacterial cell-division protein FtsZ complexed with GDP. Nature 391, 203-206 (1998).
28. Ponstingl, H., Krauhs, E., Little, M., Kempf, T., Hofer-Warbinek, R. & Ade, W. Amino acid sequence of α-and β-tubulins from pig brain: heterogeneity and regional similarity to muscle proteins. Cold Spring Harbor Symp. Quant. Biol. 46, 191-197 (1982).
29. Mitchison, T. J. Localization of an exchangeable GTP binding site at the plus end of microtubules. Science 261, 1044-1047 (1993).
30. Fan, J., Griffiths, A. D., Lockhart, A., Cross, R. A. & Amos, L. A. Microtubule minus ends can be labeled with a phage display antibody specific to α-tubulin. J. Mol. Biol. 259, 325-330 (1996).