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Genomes and Genes | Markus C WahlSummaryCountry: Germany Publications
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Publications
Structure and catalytic mechanism of eukaryotic selenocysteine synthaseOleg 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...
The spliceosome: design principles of a dynamic RNP machineMarkus C Wahl
Makromolekulare Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
Cell 136:701-18. 2009....- Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogasterMarkus 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... 
Structure and function of an RNase H domain at the heart of the spliceosomeVladimir 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...- Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding siteRalf 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... - 1.8 A bright-state structure of the reversibly switchable fluorescent protein Dronpa guides the generation of fast switching variantsAndre 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... - Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segmentRalf 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... - An unusual RNA recognition motif acts as a scaffold for multiple proteins in the pre-mRNA retention and splicing complexSimon Trowitzsch
Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
J Biol Chem 283:32317-27. 2008.... - Structural basis for reversible photoswitching in DronpaMartin 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... - Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNPSunbin 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... - Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicaseVladimir Pena
Abteilung Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
Mol Cell 35:454-66. 2009.... - Molecular basis of the light-driven switching of the photochromic fluorescent protein PadronTanja 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... - Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complexXiao 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... - Crystal structure of the Pml1p subunit of the yeast precursor mRNA retention and splicing complexSimon 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... - The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNASina 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... - Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosaVladimir 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... - Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangementsRalf 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... - The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction moduleRalf 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... - Conformational switches in winged-helix domains 1 and 2 of bacterial translation elongation factor SelBOleg 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.... - The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP proteinChristian 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... - Functional stabilization of an RNA recognition motif by a noncanonical N-terminal expansionCatharina 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... - Towards understanding selenocysteine incorporation into bacterial proteinsNiels 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... - Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activationMihaela 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... - The thermodynamic influence of trapped water molecules on a protein-ligand interactionChristian 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.... - Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptideUlrich Reidt
Abteilung für Zelluläre Biochemie, Max Planck Institut fur biophysikalische Chemie, 37077 Gottingen, Germany
J Mol Biol 331:45-56. 2003.... - Structure and mechanism of the reversible photoswitch of a fluorescent proteinMartin Andresen
Department of NanoBiophotonics, Theoretical and Computational Biophysics, and X-Ray Crystallography, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, , 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... - Oligomeric state and mode of self-association of Thermotoga maritima ribosomal stalk protein L12 in solutionPierre 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... - Structural and functional investigation of a putative archaeal selenocysteine synthaseJens 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.... - Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activitiesThomas 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... - Structure and function of the acidic ribosomal stalk proteinsMarkus 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... - Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparisonAlbrecht 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... - Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA bindingIrena 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... - Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambdaIrena 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... - CASK Functions as a Mg2+-independent neurexin kinaseKonark 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... - Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologiesDaniel 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...