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Publikationen

Originalarbeiten

• What glues a homodimer together: Systematic analysis of the stabilizing effect of an aromatic hot spot in the protein – protein interface of the tRNA-modifying enzyme Tgt.
  S. Jakobi, T.X.P. Nguyen, F. Debaene, S. Sanglier-Cianférani, K. Reuter, G. Klebe
  CS Chemical Biology, 2015, 10, 1897-1907
  
• Hot spot analysis to dissect the functional protein-protein interface of a tRNA-modifying enzyme.
  S. Jakobi, T.X.P. Nguyen, F. Debaene, A. Metz, S. Sanglier-Cianférani, K. Reuter, G. Klebe
  Proteins Struct. Funct. Bioinf., 2014, 82, 2713-2732
  
• High resolution crystal structure of Clostridium propionicum β-alanyl-CoA:ammonia lyase, a new member of the "hot dog fold" protein superfamily.
  A. Heine, G. Herrmann, T. Selmer, F. Terwesten, W. Buckel, K. Reuter
  Proteins Struct. Funct. Bioinf., 2014, 82, 2041-2053
  
• Launching spiking ligands into a protein-protein interface: a promising strategy to destabilize and break interface formation in a tRNA modifying enzyme.
  F. Immekus, L.J. Barandun, M. Betz, F. Debaene, S. Petiot, S. Sanglier-Cianferani, K. Reuter, F. Diederich, G. Klebe
  ACS Chemical Biology, 2013, 8, 1163-1178
  
• Investigation of specificity determinants in bacterial tRNA-guanine transglycosylase reveals queuine, the substrate of its eucaryotic counterpart, as inhibitor.
  I. Biela, N. Tidten-Luksch, F. Immekus, S. Glinca, T.X.P. Nguyen, H.-D. Gerber, A. Heine, G. Klebe, K. Reuter
  PLoS One, 2013, 8, e64240
  
• Synthesis of the compatible solute 5-hydroxyectoine from ectoine: Crystal structure of the non-heme iron(II)-dependent dioxygenase EctD.
  K. Reuter, M.Pittelkow, J. Bursy, A. Heine, T. Craan, E. Bremer
  PloS One, 2010, 5, e10647
  
• A crystallization screen based on alternative polymeric percipitants.
  C. Grimm, A. Chari, K. Reuter, U. Fischer
  Acta Crystallogr. Sect. D 2010, 66, 685-697
  
• An integrative approach combining noncovalent mass spectrometry, enzyme kinetics and X-ray crystallography to decipher Tgt protein-protein and protein-RNA interaction.
  T. Ritschel, C. Atmanene, K. Reuter, A. Van Dorsselaer, S. Sanglier-Cianferani, G. Klebe
  J. Mol. Biol. 2009, 393, 833-847
  
• Glutamate versus glutamine exchange swaps substrate selectivity in tRNA-guanine transglycosylase: insight into the regulation of substrate selectivity by kinetic and crystallographic studies.
  N. Tidten, B. Stengl, A. Heine, G.A. Garcia, G. Klebe, K. Reuter
  J. Mol. Biol. 2007, 374, 764-776
  
• Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase.
  C. Grimm, R. Ficner, T. Sgraja, P. Haebel, G. Klebe, K. Reuter
  Biochem. Biophys. Res. Comm. 2006, 351, 695-701
  
• Synthesis, biological evaluation, and crystallographic studies of extended guanine-based (lin-Benzoguanine) inhibitors for tRNA-guanine transglycosylase (TGT).
  E. A. Meyer, N. Donati, M. Guillot, W.B. Schweizer, F. Diederich, B. Stengl, R. Brenk, K. Reuter, G. Klebe
  Helv. Chim. Acta 2006, 89, 573-597
  
• Structural insights into the neuroprotective acting carbonyl reductase Sniffer ofDrosophila melanogaster.
  T. Sgraja, J. Ulschmid, K. Becker, S. Schneuwly, G. Klebe, K. Reuter, A. Heine
  J. Mol. Biol. 2004, 342, 1613-1624
  
• Crystallographic study of inhibitors of tRNA-guanine transglycosylase suggests a new structure-based pharmacophore for virtual screening.
  R. Brenk, E. Meyer, K. Reuter, M.T. Stubbs, G.A. Garcia, F. Diederich, G. Klebe
  J. Mol. Biol. 2004, 338, 55-75
  
• Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug design.
  R. Brenk, M.T. Stubbs, A. Heine, K. Reuter, G. Klebe
  ChemBioChem. 2003, 4, 1066-1077
  
• An essential role for aspartate 264 in catalysis by tRNA-guanine transglycosylase from Escherichia coli.
  J.D. Kittendorf, T. Sgraja, K. Reuter, G. Klebe, G.A. Garcia
  J. Biol. Chem. 2003, 278, 42369-42376
  
• From hit to lead: De novo design based on virtual screening hits of inhibitors of tRNA-guanine transglycosylase, a putative target of shigellosis therapy.
  R. Brenk, H.-D. Gerber, J.D. Kittendorf, G.A. Garcia, K. Reuter, G. Klebe
  Helv. Chim. Acta 2003, 86, 1435-1452
  
• Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modeling of its ligand bound active centre.
  C. Grimm, A. Evers, W. Buckel, C. Maerker, G. Klebe, M. Brock, K. Reuter
  J. Mol. Biol. 2003, 328, 609-621
  
• Virtual screening for submicromolar leads of Tgt based on a new unexpected binding mode detected by crystal structure analysis.
  R. Brenk, L. Naerum, U. Grädler, H.-D. Gerber, G.A. Garcia, K. Reuter, M.T. Stubbs, G. Klebe
  J. Med. Chem. 2003, 46, 1133-1143
  
• A novel recessive hyperekplexia allele GLRA1 (S231R): genotyping by MALDI-TOF mass spectrometry and functional characterization as a determinant of cellular glycine receptor trafficking.
  A. Humeny, T. Bonk, K. Becker, M. Jafari-Boroujerdi, U. Stephani, K. Reuter, C.-M. Becker
  Eur. J. Hum. Genet. 2002, 10, 188-196
  
• Crystal structure of 1-deoxy-d-xylulose-5-phosphate reductoisomerase, a crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis.
  K. Reuter, S. Sanderbrand, H. Jomaa, J. Wiesner, I. Steinbrecher, E. Beck, M. Hintz, G. Klebe, M.T. Stubbs
  J. Biol. Chem. 2002, 277, 5378-5384
  
• A new target for Shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanin transglycosylase.
  U. Grädler, H.D. Gerber, D.A.M. Goodenough-Lashua, G.A. Garcia, R. Ficner, K. Reuter, M.T. Stubbs, G. Klebe
  J. Mol. Biol. 2001, 306, 455-467
  
• The crystal structure of 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family.
  C. Grimm, E. Maser, E. Möbus, G. Klebe, K. Reuter, F. Ficner
  J. Biol. Chem. 2000, 275, 41333-41339
  
• Screening orthologs as an important variable in crystallization: preliminary X-ray diffraction studies of the tRNA-modifying enzyme S-adenosyl-methionine:tRNA ribosyl transferase/isomerase.
  C. Grimm, G. Klebe, R. Ficner, K. Reuter
  Acta Crystallogr. Sect. D 2000, 56, 484-488
  
• Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin.
  U. Reidt, K. Reuter, T. Achsel, D. Ingelfinger, R. Lührmann, R. Ficner
  J. Biol. Chem. 2000, 275, 7439-7442
  
• Crystal structure of the surfactin synthetase activating enzyme Sfp: a prototype of the 4´-phosphopantetheinyl transferase superfamily.
  K. Reuter, M.R. Mofid, M.A. Marahiel, R. Ficner
  EMBO J. 1999, 18, 6823-6831
  
• Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein.
  K. Reuter, S. Nottrott, P. Fabrizio, R. Lührmann, R. Ficner
  J. Mol. Biol. 1999, 249, 515-525
  
• Mutagenesis and crystallographic studies of Zymomonas mobils tRNA-guanine transglycosylase to elucidate the role of serine¹⁰³ for enzymatic activity.
  U. Grädler, R. Ficner, G.A. Garcia, M.T. Stubbs, G. Klebe, K. Reuter
  FEBS Lett. 1999, 454, 142-146
  
• Crystallization and preliminary crystallographic studies of Sfp: a phosphopantetheinyl transferase of modular peptide synthetases.
  M.R. Mofid, M.A. Marahiel, R. Ficner, K. Reuter
  Acta Crystallogr. Sect. D 1999, 55, 1098-1100
  
• Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human spliceosomal protein U5-15kD.
  K. Reuter, R. Ficner
  Acta Crystallogr. Sect. D 1999, 55, 888-890
  
• Cloning and functional characterization of the genes encoding 3-dehydroquinate synthase (aroB) and tRNA-guanine transglycosylase (tgt) from Helicobacter pylori.
  S. Bereswill, F. Faßbinder, C. Völzing, R. Haas, K. Reuter, R. Ficner, M. Kist
  Med. Microbiol. Immunol. 1997, 186, 125-134
  
• Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase reveal aspartate¹⁰² as the active site nucleophile.
  C. Romier, K. Reuter, D. Suck, R. Ficner
  Biochemistry 1996, 35, 15734-15739
  
• Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange.
  C. Romier, K. Reuter, D. Suck, R. Ficner
  EMBO J. 1996, 15, 2850-2857
  
• Purification, crystallization, and preliminary X-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis.
  C. Romier, R. Ficner, K. Reuter, D. Suck
  Proteins: Struct. Funct. Genet. 1996, 24, 516-519
  
• Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzyme.
  K. Reuter, R. Ficner
  J. Bacteriol. 1995, 177, 5284-5288
  
• Serine⁹⁰ is required for enzymic activity by tRNA-guanine transglycosylase from Escherichia coli.
  K. Reuter, S. Chong, F. Ullrich, H. Kersten, G.A. Garcia
  Biochemistry 1994, 33, 7041-7046
  
• Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eucaryotes.
  K. Reuter, R. Slany, F. Ullrich, H. Kersten
  J. Bacteriol. 1991, 173, 2256-2264
  

Übersichtsartikel

• Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanism.
  B. Stengl, K. Reuter, G. Klebe
  ChemBioChem. 2005, 6, 1926-1939
  
• Neue Konzepte zur Arzneistoffsuche und Synthese.
  W. Diederich, P. Haebel, A. Heine, K. Reuter, C. Sotriffer, G. Klebe
  LaborPraxis 2004, 28, 24-26
  
• 3α-Hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: biological significance, three-dimensional structure and gene regulation.
  E. Maser, G. Xiong, C. Grimm, R. Ficner, K. Reuter
  Chem.-Biol. Interact. 2000, 130, 707-722