Markus C Wahl

Summary

Country: Germany

Publications

  1. ncbi request reprint Structure and catalytic mechanism of eukaryotic selenocysteine synthase
    Oleg M Ganichkin
    Max Planck Institut fur biophysikalische Chemie, Zelluläre Biochemie Makromolekulare Röntgenkristallographie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Biol Chem 283:5849-65. 2008
  2. pmc The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein
    Christian M Stegmann
    Max Planck Institut fur biophysikalische Chemie, Zelluläre Biochemie Makromolekulare Röntgenkristallographie, Gottingen, Germany
    PLoS ONE 5:e10013. 2010
  3. doi request reprint The spliceosome: design principles of a dynamic RNP machine
    Markus C Wahl
    Makromolekulare Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    Cell 136:701-18. 2009
  4. ncbi request reprint Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster
    Markus C Wahl
    Max Planck Institut fur biophysikalische Chemie, Arbeitsgruppe Röntgenkristallographie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Mol Biol 345:1119-30. 2005
  5. pmc Structure and function of an RNase H domain at the heart of the spliceosome
    Vladimir Pena
    Abteilung Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Gottingen, Germany
    EMBO J 27:2929-40. 2008
  6. pmc 1.8 A bright-state structure of the reversibly switchable fluorescent protein Dronpa guides the generation of fast switching variants
    Andre C Stiel
    Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Biochem J 402:35-42. 2007
  7. ncbi request reprint Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site
    Ralf Jauch
    Max Planck Institut fur biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Am Fassberg 11, 37077 Gottingen, Germany
    Structure 13:1559-68. 2005
  8. pmc Molecular basis of the light-driven switching of the photochromic fluorescent protein Padron
    Tanja Brakemann
    Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    J Biol Chem 285:14603-9. 2010
  9. pmc Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment
    Ralf Jauch
    Max Planck Institut fur biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Gottingen, Germany
    EMBO J 25:4020-32. 2006
  10. doi request reprint An unusual RNA recognition motif acts as a scaffold for multiple proteins in the pre-mRNA retention and splicing complex
    Simon Trowitzsch
    Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Biol Chem 283:32317-27. 2008

Collaborators

Detail Information

Publications38

  1. ncbi request reprint Structure and catalytic mechanism of eukaryotic selenocysteine synthase
    Oleg M Ganichkin
    Max Planck Institut fur biophysikalische Chemie, Zelluläre Biochemie Makromolekulare Röntgenkristallographie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Biol Chem 283:5849-65. 2008
    ..Based on these results and on the activity profiles of mechanism-based inhibitors, we offer a detailed reaction mechanism for the enzyme...
  2. pmc The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein
    Christian M Stegmann
    Max Planck Institut fur biophysikalische Chemie, Zelluläre Biochemie Makromolekulare Röntgenkristallographie, Gottingen, Germany
    PLoS ONE 5:e10013. 2010
    ..The peptidyl-prolyl cis/trans isomerase PPIL1 is a component of the human spliceosome and binds to the spliceosomal SKIP protein via a binding site distinct from its active site...
  3. doi request reprint The spliceosome: design principles of a dynamic RNP machine
    Markus C Wahl
    Makromolekulare Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    Cell 136:701-18. 2009
    ....
  4. ncbi request reprint Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster
    Markus C Wahl
    Max Planck Institut fur biophysikalische Chemie, Arbeitsgruppe Röntgenkristallographie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Mol Biol 345:1119-30. 2005
    ..In human Trx, oxidative dimerization has been demonstrated in vitro. Therefore, this finding may indicate a difference in redox control of GR-free and GR-containing organisms...
  5. pmc Structure and function of an RNase H domain at the heart of the spliceosome
    Vladimir Pena
    Abteilung Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Gottingen, Germany
    EMBO J 27:2929-40. 2008
    ..These data suggest that Prp8 employs an RNase H domain to help assemble and stabilize the spliceosomal catalytic core, coordinate the activities of other splicing factors and possibly participate in chemical catalysis of splicing...
  6. pmc 1.8 A bright-state structure of the reversibly switchable fluorescent protein Dronpa guides the generation of fast switching variants
    Andre C Stiel
    Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Biochem J 402:35-42. 2007
    ..The findings reported in the present study support the view that a cis-trans isomerization is one of the key events common to the switching mechanism in RSFPs...
  7. ncbi request reprint Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site
    Ralf Jauch
    Max Planck Institut fur biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Am Fassberg 11, 37077 Gottingen, Germany
    Structure 13:1559-68. 2005
    ..The results suggest that the ATP binding pocket and the activation segment of Mnk2 require conformational switches to provide kinase activity...
  8. pmc Molecular basis of the light-driven switching of the photochromic fluorescent protein Padron
    Tanja Brakemann
    Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    J Biol Chem 285:14603-9. 2010
    ..Distinct absorption cross-sections for the switching wavelengths in the fluorescent and the nonfluorescent state are not essential for efficient photochromism in fluorescent proteins, although they may facilitate the switching process...
  9. pmc Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment
    Ralf Jauch
    Max Planck Institut fur biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Gottingen, Germany
    EMBO J 25:4020-32. 2006
    ..Our data suggest a novel regulatory mechanism specific for the Mnk subfamily...
  10. doi request reprint An unusual RNA recognition motif acts as a scaffold for multiple proteins in the pre-mRNA retention and splicing complex
    Simon Trowitzsch
    Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Biol Chem 283:32317-27. 2008
    ....
  11. ncbi request reprint Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP
    Sunbin Liu
    Abteilung Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    Science 316:115-20. 2007
    ..Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation...
  12. doi request reprint Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase
    Vladimir Pena
    Abteilung Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    Mol Cell 35:454-66. 2009
    ....
  13. pmc Structural basis for reversible photoswitching in Dronpa
    Martin Andresen
    Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Proc Natl Acad Sci U S A 104:13005-9. 2007
    ..We suggest a comprehensive model for the light-induced switching mechanism, connecting a cascade of structural rearrangements with different protonation states of the chromophore...
  14. doi request reprint Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8
    Sina Mozaffari-Jovin
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    Science 341:80-4. 2013
    ..Our data show how a Ski2-like RNA helicase can be reversibly inhibited by a protein cofactor that directly competes with RNA substrate binding. ..
  15. pmc Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex
    Xiao Luo
    Research Group X ray Crystallography, Max Planck Institute for Biophysical Chemistry, D 37077 Gottingen, Germany
    Mol Cell 32:791-802. 2008
    ..These data demonstrate that S10 and NusB together form a BoxA-binding module, that NusB facilitates entry of S10 into the transcription machinery, and that S10 represents a central hub in processive antitermination...
  16. doi request reprint Crystal structure of the Pml1p subunit of the yeast precursor mRNA retention and splicing complex
    Simon Trowitzsch
    Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Mol Biol 385:531-41. 2009
    ..Our results show that in the RES complex, an FHA domain of Pml1p is flexibly tethered via an unstructured N-terminal region to Snu17p...
  17. pmc The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNA
    Sina Mozaffari-Jovin
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, D 37077 Gottingen, Germany
    Genes Dev 26:2422-34. 2012
    ..Our results provide insights into the mechanism whereby Brr2 unwinds U4/U6 and show how this activity is potentially regulated prior to spliceosome activation...
  18. ncbi request reprint Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements
    Ralf Jauch
    Max Planck Institut fur biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Am Fassberg 11, D 37077 Gottingen, Germany
    J Biol Chem 280:15131-40. 2005
    ..Phylogenetic structure comparisons suggest that the present results are relevant for designing species-specific antibiotics...
  19. ncbi request reprint Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa
    Vladimir Pena
    AG Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    Mol Cell 25:615-24. 2007
    ..We conclude that the expanded Prp8 Jab1/MPN domain represents a pseudoenzyme converted into a protein-protein interaction platform and that dysfunction of this platform underlies Retinitis pigmentosa...
  20. ncbi request reprint Conformational switches in winged-helix domains 1 and 2 of bacterial translation elongation factor SelB
    Oleg Ganichkin
    Max Planck Institut fur biophysikalische Chemie, Makromolekulare Röntgenkristallographie, Am Fassberg 11, D 37077 Gottingen, Germany
    Acta Crystallogr D Biol Crystallogr 63:1075-81. 2007
    ....
  21. ncbi request reprint The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction module
    Ralf Jauch
    Max Planck Institut fur biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Röntgenkristallographie, Am Fassberg 11, D 37077 Gottingen, Germany
    Structure 11:1393-402. 2003
    ..The results indicate that ZAD provides a novel protein-protein interaction module that characterizes a large family of insect transcription factors...
  22. pmc Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies
    Daniel Zwilling
    Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    EMBO J 26:9-18. 2007
    ..We conclude that homotypic fusion reactions may proceed with multiple SNARE topologies, suggesting that the conserved SNARE structure allows for flexibility in the initial interactions needed for fusion...
  23. doi request reprint A reversibly photoswitchable GFP-like protein with fluorescence excitation decoupled from switching
    Tanja Brakemann
    Max Planck Institute for Biophysical Chemistry, Department of NanoBiophotonics, Gottingen, Germany
    Nat Biotechnol 29:942-7. 2011
    ..The switching properties of Dreiklang enable far-field fluorescence nanoscopy in living mammalian cells using both a coordinate-targeted and a stochastic single molecule switching approach...
  24. ncbi request reprint Towards understanding selenocysteine incorporation into bacterial proteins
    Niels Fischer
    3D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, D 37077 Gottingen, Germany
    Biol Chem 388:1061-7. 2007
    ..The results indicate that mthSelA forms a homodecamer that has a ring-like structure with five bilobed wings, similar to the structure of the E. coli complex determined previously...
  25. pmc Functional stabilization of an RNA recognition motif by a noncanonical N-terminal expansion
    Catharina Netter
    Max Planck Institut fur biophysikalische Chemie, D 37077 Gottingen, Germany
    RNA 15:1305-13. 2009
    ..These results demonstrate that the 65K C-terminal RRM is augmented by an N-terminal element that confers stability to the domain, and thereby facilitates stable RNA binding...
  26. ncbi request reprint Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide
    Ulrich Reidt
    Abteilung für Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, 37077 Gottingen, Germany
    J Mol Biol 331:45-56. 2003
    ....
  27. doi request reprint The thermodynamic influence of trapped water molecules on a protein-ligand interaction
    Christian M Stegmann
    Research Group X ray Crystallography, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Angew Chem Int Ed Engl 48:5207-10. 2009
    ....
  28. pmc Functional organization of the Sm core in the crystal structure of human U1 snRNP
    Gert Weber
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    EMBO J 29:4172-84. 2010
    ..The intricate, multi-layered interplay of proteins and RNA rationalizes the hierarchical assembly of U snRNPs in vitro and in vivo...
  29. ncbi request reprint Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation
    Mihaela Diaconu
    Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    Cell 121:991-1004. 2005
    ..Highly mobile L7/12 C-terminal domains promote recruitment of translation factors to the ribosome and stimulate GTP hydrolysis by the ribosome bound factors through stabilization of their active GTPase conformation...
  30. pmc Structure and mechanism of the reversible photoswitch of a fluorescent protein
    Martin Andresen
    Department of NanoBiophotonics, Theoretical and Computational Biophysics, and X Ray Crystallography, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Proc Natl Acad Sci U S A 102:13070-4. 2005
    ..Reversible photoswitching of the protein chromophore system within intact crystals also constitutes a step toward the use of fluorescent proteins in three-dimensional data recording...
  31. ncbi request reprint Structural and functional investigation of a putative archaeal selenocysteine synthase
    Jens T Kaiser
    Division of Chemistry and Chemical Engineering, California Institute of Technology, M C 114 96, Pasadena, California 91125, USA
    Biochemistry 44:13315-27. 2005
    ....
  32. pmc Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities
    Thomas Steiner
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    EMBO J 21:4641-53. 2002
    ..The results strongly argue that both protein and nucleic acid contacts are important for NusG's functions and that the factor can act as an adaptor mediating indirect protein-nucleic acid associations...
  33. ncbi request reprint Oligomeric state and mode of self-association of Thermotoga maritima ribosomal stalk protein L12 in solution
    Pierre D J Moens
    School of Biological, Biomedical, and Molecular Sciences, The University of New England, Armidale, New South Wales 2351, Australia
    Biochemistry 44:3298-305. 2005
    ..coli system. The exchange rate increases with increasing temperature and approaches the one observed for the E. coli system at 50 degrees C. Possible factors responsible for this difference are discussed...
  34. ncbi request reprint Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison
    Albrecht Messerschmidt
    Max Planck Institut for Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Planegg Martinsried, Germany
    Biol Chem 384:373-86. 2003
    ..In methionine gamma-lyase a hydrophic patch operates as recognition site for the methyl group of the methionine substrate...
  35. ncbi request reprint Structure and function of the acidic ribosomal stalk proteins
    Markus C Wahl
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Curr Protein Pept Sci 3:93-106. 2002
    ..The discrepancies between the crystal structures and results from other physico-chemical methods may partly be a consequence of the dynamic functions of the proteins, necessitating a high flexibility...
  36. pmc Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambda
    Irena Bonin
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 101:13762-7. 2004
    ..Contrary to the RNA polymerase alpha subunit, lambdaN binding does not stimulate RNA interaction of NusA. The results demonstrate that lambdaN serves as a scaffold to closely oppose NusA and the mRNA in antitermination complexes...
  37. pmc CASK Functions as a Mg2+-independent neurexin kinase
    Konark Mukherjee
    Department of Neuroscience, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390 9111, USA
    Cell 133:328-39. 2008
    ..Moreover, our study suggests that other pseudokinases (10% of the kinome) could also be catalytically active...
  38. pmc Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding
    Irena Bonin
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Biochem J 383:419-28. 2004
    ..Therefore, in certain organisms, dimerization may be employed to package NusB in an inactive form until recruitment into antitermination complexes...