Deciphering the alphabet of G proteins: The structure of the α, β, γ heterotrimer

Structure

Volumn 4, Issue 4, 1996, Pages 357-361

  Wittinghofer, Alfred ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE;

BIOLOGICAL MODEL; CHEMISTRY; METABOLISM; PROTEIN CONFORMATION; REVIEW;

GTP-BINDING PROTEINS; GUANOSINE TRIPHOSPHATE; MODELS, BIOLOGICAL; PROTEIN CONFORMATION;

EID: 0030584675     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00040-8     Document Type: Article

References (38)

1. Arai, K-i., Kawakita, M. & Kaziro, Y. (1974). Studies on the polypeptide elongation factors from E. coli. J. Biochem. 76, 283-292.
2. Phr, EF-Tu, and a GTP analog. Science 270, 1464-1472.
3. Leberman, R., Schulz, G.E. & Suck, D. (1981). Crystallization and preliminary X-ray diffraction data of the EF-Tu·EF-Ts (EF-T) complex of Escherichia coli. FEBS Lett. 124, 279-281.
4. Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S. & Leberman, R. (1996). The structure of the Escherichia coli EF-Tu·EF-Ts complex at 1.5 Å resolution. Nature 379, 511-518.
5. Daum, G., Eisenmann-Tappe, I., Fries, H.-W., Troppmair, J. & Rapp, U.R. (1994). The ins and cuts of Raf kinases. Trends Biol. Sci. 19, 474-480.
6. Nassar, N., Horn, G., Herrmann, C., Scherer, A., McCormick, F. & Wittinghofer, A. (1995). The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 375, 554-560.
7. Derrick, J.P. & Wigley, D.B. (1992). Crystal structure of a streptococcal protein G domain bound to an Fab fragment. Nature 359, 752-754.
8. Lian, L.-Y., Barsukov, I.L., Derrick, J.P. & Roberts, G.C.K. (1994). Mapping the interactions between streptococcal protein G and the Fab fragment of IgG in solution. Nat. Struct. Biol. 1, 355-357.
9. Yu, H. & Schreiber, S.L. (1995). Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface. Nature 376, 788-791.
10. Noel, J.P., Hamm, H.E. & Sigler, P.B. (1993). The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366, 654-663.
11. Lambright, D.G., Noel, J.P., Hamm, H.E. & Sigler, P.B. (1994). Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369, 621-628.
12. iα1 and the mechanism of GTP hydrolysis, Science 265, 1405-1412.
13. iα1 induced by GTP hydrolysis. Science 270, 954-960.
14. 4. Nature 372, 276-279.
15. 1γ2. Cell 83, 1047-1058.
16. Lambright, D.G., Sondek, J., Bohm, A., Skiba, N.P., Hamm, H.E. & Sigler, P.B. (1996). The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 379, 311-319.
17. Conklin, B.R. & Bourne, H.R. (1993). Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors. Cell 73, 631-641.
18. Pai, E.F., Kabsch, W., Krengel, U., Holmes, K.C., John, J. & Wittinghofer, A. (1989). Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341, 209-214.
19. Milburn, M.V., et al., & Kim S.-H. (1990). Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 247, 939-945.
20. Amor, J.C., Harrison, D.H., Kahn, R.A. & Ringe, D. (1994). Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372, 704-708.
21. Scheffzek, K., Klebe, C., Fritz-Wolf, K., Kabsch, W. & Wittinghofer, A. (1995). Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature 374, 378-381.
22. LaCour, T.F.M., Nyborg, J., Thirup, S. & Clark, B.F.C. (1985). Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. EMBO J. 4, 2385-2388.
23. Jurnak, F. (1985). Structure of the GDP domain of EF-Tu and location of amino acids homologous to ras oncogene proteins. Science 230, 32-36.
24. Berchtold, H., Reshetnikova, L., Reiser, C.P.A., Schirmer, N.K., Sprinzl, M. & Hilgenfeld, R. (1993). Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature 365, 126-132.
25. Czworkowski, J., Wang, J., Steitz, T.A. & Moore, P.B. (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13, 3661-3668.
26. Ævarsson, A., et al., & Liljas, L. (1994). Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J. 13, 3669-3677.
27. Wittinghofer, A. & Pai, E. (1991). The structure of ras protein: a model for a universal molecular switch. Trends Biol. Sci. 16, 383-387.
28. Wittinghofer, A., Pai, E.F. & Goody, R.S. (1993). Structural and mechanistic aspects of the GTPase reaction of H-ras p21. In GTPases in Biology I. (Dickey, B.F. & Birnbauer, L., eds), pp. 195-211, Springer-Verlag, Berlin, Heidelberg and New York.
29. ras and other GTP-binding proteins. Nature Struct. Biol. 2, 36-44.
30. Goody, R.S. (1994). How G proteins turn off. Nature 372, 220-221.
31. A protein βγ dimer at 2.1 Å resolution. Nature 379, 369-374.
32. Neer, E.J., Schmidt, C.J., Nambudripad, R. & Smith, T.F. (1994). The ancient regulatory-protein family of WD-repeat proteins. Nature 371, 297-300.
33. Fong, H.K.W., et al., & Simon, M.I. (1986). Repetitive segmental structure of the transducin beta subunit: Homology with the CDC4 gene and identification of related mRNAs. Proc. Natl. Acad. Sci. USA 83, 2162-2166.
34. Peifer, M., Berg, S. & Reynolds, A.B. (1994). A repeating amino acid motif shared by proteins with diverse cellular roles. Cell 76, 789-791.
35. Lupas, A., Van Dyke, M. & Stock, J. (1991). Predicting coiled coils from protein sequences. Science 252, 1162-1164.
36. Garristen, A., Van Galen, P.J.M. & Simonds, W.F. (1993). The N-terminal coiled-coil domain of β is essential for γ association: a model for G-protein βγ subunit interaction. Proc. Natl. Acad. Sci. USA 90, 7706-7710.
37. Higgins, J.B. & Casey, P.J. J. (1994). In vitro processing of recombinant G protein -y subunits. Biol. Chem. 269, 9067-9073.
38. Rens-Domiano, S. & Hamm, H.E. (1995). Structural and functional relationships of heterotrimeric G-proteins. FASEB J. 9, 1059-1066.