Grüber, Gerhard


Selected Publications

  1. Gayen, S., Balakrishna, A. M., Biuković, G., Yulei, W. and Grüber, G. (2008) Identification of critical residues of subunit H in its interaction with subunit E of the A-ATP synthase from Methanocaldococcus jannaschii. FEBS Journal, 275, 1803-1812
  2. Thaker, Y. R., Roessle, M. and Grüber, G. (2007) The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein. J. Bioenerg. Biomembr. 39, 275-289
  3. Biuković, G., Rössle, M., Gayen, S., Mu, Y., and Grüber, G. (2007) Small-angle X-ray scattering reveals the solution structure of the peripheral stalk subunit H of the A1AO ATP synthase from Methanocaldococcus jannaschii and its binding to the catalytic A subunit. Biochemistry 46, 2070-2078
  4. Schäfer, I., Rössle, M., Biuković G., Müller, V. and Grüber, G. (2006) Structural and functional analysis of the coupling subunit F in solution and topological arrangement of the stalk domains of the methanogenic A1AO ATPsynthase. J. Bioenerg. Biomembr. 38, 83-92
  5. Schäfer, I., Bailer, S. M., Düser, M. G., Börsch, M., Ricardo, A. B., Stock, D., and Grüber, G. (2006) Crystal structure of the archaeal A1AO ATPsynthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1AO subunits A and B. J. Mol. Biol. 358, 725-740
  6. Grüber, G. (2005) The coupling of relative movements of subunit C to the reversible disassembly of the V1 and VO domain in the vacuolar ATPase. Biochem. Soc. Trans. 33 (4), 300-303
  7. Chaban, Y. L. Juliano, S., Boekema E. J., and Grüber, G. (2005) Interaction between subunit C (Vma5p) of the yeast vacuolar ATPase and the stalk of the C-depleted V1 ATPase from Manduca sexta Midgut. Biochim. Biophys. Acta 1708, 196-200
  8. Armbrüster, A. Hohn, C., Hermesdorf, A., Schumacher, K., Börsch, M. and Grüber, G. (2005) Evidence for Major Structural Changes in subunit C of the vacuolar ATPase due to Nucleotide binding. FEBS Lett. 579, 1961-1967
  9. Coskun, Ü., Chaban, Y. L., Lingl, A., Müller, V., Keegstra, W., Boekema, E. J. and Grüber, G. (2004) Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jannaschii visualized by electron microscopy. J. Biol. Chem. 279, 38644-38648
  10. Chaban, Y. L., Coskun, Ü., Keegstra, W., Oostergetel, G. T., Boekema, E. J. and Grüber, G. (2004) Structural characterization of an ATPase active F1-/V1-ATPase hybrid complex. J. Biol. Chem. 279, 47866-47870
  11. Coskun, Ü., Radermacher, M., Müller, V., Ruiz, T. and Grüber, G. (2004) Three-dimensional organization of the A1 ATPase from Methanosacina mazei Gö1. J. Biol. Chem. 279, 22759-22764
  12. Grüber, G. (2003) Frontiers in Vacuolar ATPase Research. In: Minireview Series: V-type ATPase: News and Views of a Marvelous Ion Pump (G. Grüber, Series Editor). J. Bioenerg. Biomembr. 35, 277-280
  13. Müller, V. and Grüber, G. (2003) ATP synthases from archaea and bacteria: common principles and differences. Cell. Mol. Life Sci. 60, 474-494
  14. Rizzo, V. F., Coskun, Ü., Radermacher, M., Ruiz, T., Armbrüster, A. and Grüber, G., (2003) Resolution of the V1-ATPase from Manduca sexta into subcomplexes and visualization of an ATPase active A3B3EG-complex by electron microscopy. J. Biol. Chem. 278, 270-275
  15. Radermacher, M., Ruiz, T., Wieczorek, H. and Grüber, G. (2001) Three-Dimensional Electron Microscopy Reveals The Structure Of The V1-ATPase. J. Struct. Biol. 135, 26-37
  16. Grüber, G., Svergun, D.I., Coskun, Ü., Lemker, T., Koch, M.H.J., Schägger, H. and Müller, V. (2000) Structural insights into the A1 ATPase from Methanosarcina mazei Gö1. Biochemistry 40, 1890-1896
  17. Svergun, D.I., Bećirević, A., Schrempf, H., Koch, M.H.J. and Grüber, G. (2000) Solution structure and conformational changes of the Streptomyces Chitin-Binding Protein (CHB1). Biochemistry 39, 10677-10683
  18. Hausrath, A.C., Grüber, G., Matthews, B.W. and Capaldi, R.A. (1999) Structural Features of the γ Subunit of the Escherichia coli F1 ATPase Revealed by a 4.4 Å Resolution Map Obtained by X-ray Crystallography. Proc. Natl. Acad. Sci. USA 96, 13697-13702