3D structure of a binary ROP-PRONE complex: The final intermediate for a complete set of molecular snapshots of the RopGEF reaction

Biological Chemistry

Volumn 390, Issue 5-6, 2009, Pages 427-435

  Thomas, Christoph ^a,c   Fricke, Inka ^a,b   Weyand, Michael ^b   Berken, Antje ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b CHEMICAL GENOMICS CENTRE OF THE MAX PLANCK SOCIETY   (Germany)

^c STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

G protein; Nucleotide association; P loop; RAC; Rho; Switch

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE BINDING PROTEIN; PLANT SPECIFIC ROP NUCLEOTIDE EXCHANGE PROTEIN; RHO FACTOR; RHO PROTEIN OF PLANT; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; MOLECULAR INTERACTION; MOLECULAR MODEL; MOLECULAR STABILITY; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GUANINE NUCLEOTIDE EXCHANGE FACTORS; GUANOSINE DIPHOSPHATE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RHO GTP-BINDING PROTEINS;

EID: 67649617071     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2009.049     Document Type: Article

References (35)

1. Berken, A. (2006). ROPs in the spotlight of plant signal transduction. Cell. Mol. Life Sci. 63, 2446-2459.
2. Berken, A. and Wittinghofer, A. (2008). Structure and function of Rho-type molecular switches in plants. Plant Physiol. Biochem. 46, 380-393.
3. Berken, A., Thomas, C., and Wittinghofer, A. (2005). A new family of RhoGEFs activates the Rop molecular switch in plants. Nature 436, 1176-1180.
4. Boriack-Sjodin, P.A., Margarit, S.M., Bar-Sagi, D., and Kuriyan, J. (1998). The structural basis of the activation of Ras by Sos. Nature 394, 337-343.
5. Buchwald, G., Friebel, A., Galán, J.E., Hardt, W.D., Wittinghofer, A., and Scheffzek, K. (2002). Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE. EMBO J. 21, 3286-3295.
6. Cherfils, J. and Chardin, P. (1999). GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem. Sci. 24, 306-311.
7. Christensen, T.M., Vejlupkova, Z., Sharma, Y.K., Arthur, K.M., Spatafora, J.W., Albright, C.A., Meeley, R.B., Duvick, J.P., Quatrano, R.S., and Fowler, J.E. (2003). Conserved subgroups and developmental regulation in the monocot rop gene family. Plant Physiol. 133, 1791-1808.
8. DeLano, W.L. (2002). The PyMOL Molecular Graphics System (San Carlos, CA, USA: DeLano Scientific).
9. Diederichs, K. and Karplus, P.A. (1997). Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat. Struct. Biol. 4, 269-275.
10. Emsley, P. and Cowton, K. (2004). Coot: model-building tool for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132.
11. Fricke, I. and Berken, A. (2009). Molecular basis for the substrate specificity of plant guanine nucleotide exchange factors for ROP. FEBS Lett. 583, 75-80.
12. Gasper, R., Thomas, C., Ahmadian, M.R., and Wittinghofer, A. (2008). The role of the conserved switch II glutamate in guanine nucleotide exchange factor-mediated nucleotide exchange of GTP-binding proteins. J. Mol. Biol. 379, 51-63.
13. Goldberg, J. (1998). Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237-248.
14. Gu, Y., Li, S., Lord, E.M., and Yang, Z. (2006). Members of a novel class of Arabidopsis Rho guanine nucleotide exchange factors control Rho GTPase-dependent polar growth. Plant Cell 18, 366-381.
15. Haeusler, L.C., Blumenstein, L., Stege, P., Dvorsky, R., and Ahmadian, M.R. (2003). Comparative functional analysis of Rac GTPases. FEBS Lett. 555, 556-560.
16. John, J., Sohmen, R., Feuerstein, J., Linke, R., Wittinghofer, A., and Goody, R.S. (1990). Kinetics of interaction of nucleotides with nucleotide-free H-ras p21. Biochemistry 29, 6058-6065.
17. Kabsch, W. (1993). Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800.
18. Klebe, C., Prinz, H., Wittinghofer, A., and Goody, R.S. (1995). The kinetic mechanism of Ran-nucleotide exchange catalyzed by RCC1. Biochemistry 34, 12543-12552.
19. Lenzen, C., Cool, R.H., and Wittinghofer, A. (1995). Analysis of intrinsic and Cdc25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements. Methods Enzymol. 255, 95-109.
20. Mm.. Biochemistry 37, 7420-7430.
21. Lin, R., Bagrodia, S., Cerione, R., and Manor, D. (1997). A novel Cdc42Hs mutant induces cellular transformation. Curr. Biol. 7, 794-797.
22. Mossessova, E., Corpina, R.A., and Goldberg, J. (2003). Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism. Mol. Cell 12, 1403-1411.
23. Reinstein, J., Schlichting, I., Frech, M., Goody, R.S., and Wittinghofer, A. (1991). p21 with a phenylalanine 28-leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties. J. Biol. Chem. 266, 17700-17706.
24. Renault, L., Kuhlmann, J., Henkel, A., and Wittinghofer, A. (2001). Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Cell 105, 245-255.
25. Renault, L., Guibert, B., and Cherfils, J. (2003). Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 426, 525-530.
26. Rensland, H., John, J., Linke, R., Simon, I., Schlichting, I., Wittinghofer, A., and Goody, R.S. (1995). Substrate and product structural requirements for binding of nucleotides to H-ras p21: the mechanism of discrimination between guanosine and adenosine nucleotides. Biochemistry 34, 593-599.
27. Rossman, K.L., Worthylake, D.K., Snyder, J.T., Siderovski, D.P., Campbell, S.L., and Sondek, J. (2002). A crystallographic view of interactions between Dbs und Cdc42: PH domain-assisted guanine nucleotide exchange. EMBO J. 21, 1315-1326.
28. Simon, I., Zerial, M., and Goody, R.S. (1996). Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions. J. Biol. Chem. 271, 20470-20478.
29. Sørmo, C.G., Leiros, I., Brembu, T., Winge, P., Os, V., and Bones, A.M. (2006). The crystal structure of Arabidopsis thaliana RAC7/ROP9: the first RAS superfamily GTPase from the plant kingdom. Phytochemistry 67, 2332-2340.
30. Thomas, C., Fricke, I., Scrima, A., Berken, A., and Wittinghofer, A. (2007). Structural evidence for a common intermediate in small G protein-GEF reactions. Mol. Cell 25, 141-149.
31. Vetter, I.R. and Wittinghofer, A. (2001). The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304.
32. Wei, Y., Zhang, Y., Derewenda, U., Liu, X., Minor, W., Nakamoto, R.K., Somlyo, A.V., Somlyo, A.P., and Derewenda, Z.S. (1997). Crystal structure of RhoA-GDP and its functional implications. Nat. Struct. Biol. 4, 699-703.
33. Wennerberg, K., Rossman, K.L., and Der, C.J. (2005). The Ras superfamily at a glance. J. Cell Sci. 118, 843-846.
34. Worthylake, D.K., Rossman, K.L., and Sondek, J. (2000). Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature 408, 682-688.
35. Yang, Z. and Fu, Y. (2007). ROP/RAC GTPase signaling. Curr. Opin. Plant Biol. 10, 490-494.