Research Topics
| tRNA guanine transglycosylaseSummaryGene Symbol: tRNA guanine transglycosylase Description: queuine tRNA-ribosyltransferase Species: Top Publications
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Publications
Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilisK B Shark
School of Biological Sciences, University of Nebraska, Lincoln 68588 0118
FEMS Microbiol Lett 75:19-26. 1992..coli enzyme. Two genes located upstream of lig were identified as tgt, encoding tRNA guanine transglycosylase and uvrB, encoding the beta subunit of excision endonuclease...
Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer formation upon substrate bindingBernhard Stengl
Institut fur Pharmazeutische Chemie, Philipps Universitat Marburg, Marbacher Weg 6, 35032 Marburg, Germany
J Mol Biol 370:492-511. 2007..It is hypothesized that one unit of the dimer performs the catalytic reaction whereas the second is required to recognize and properly orient the bound tRNA for the catalytic reaction...
Crystallographic study of inhibitors of tRNA-guanine transglycosylase suggests a new structure-based pharmacophore for virtual screeningRuth Brenk
Institut fur Pharmazeutische Chemie, Philipps Universitat Marburg, Marbacher Weg 6, 35032 Marburg, Germany
J Mol Biol 338:55-75. 2004..A virtual screening has been performed based on this pharmacophore hypothesis and several new inhibitors of micromolar binding affinity with new skeletons have been discovered...
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 designRuth Brenk
Institut fur Pharmazeutische Chemie, Philipps Universitat Marburg, Marbacher Weg 6, 35032 Marburg, Germany
Chembiochem 4:1066-77. 2003..In consequence, full understanding of this plasticity can be exploited for drug design...
Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediateWei Xie
Department of Biochemistry, School of Molecular and Cellular Biology, University of Illinois at Urbana Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA
Nat Struct Biol 10:781-8. 2003Prokaryotic tRNA guanine transglycosylase (TGT) catalyzes replacement of guanine (G) by 7-aminomethyl-7-deazaguanine (PreQ1) at the wobble position of four specific tRNAs...
An essential role for aspartate 264 in catalysis by tRNA-guanine transglycosylase from Escherichia coliJeffrey D Kittendorf
Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, 428 Chuirch Street, Ann Arbor, MI 48109 1065, USA
J Biol Chem 278:42369-76. 2003..The results of these studies support two roles for aspartate 264 in catalysis by TGT, protonation of the leaving guanine and deprotonation of the incoming preQ1...
Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysisRuth Brenk
Institut fur Pharmazeutische Chemie, Philipps Universitat Marburg, Marbacher Weg 6, 35032 Marburg, Germany
J Med Chem 46:1133-43. 2003..All nine tested inhibitors being representatives of these classes showed activity in the micromolar range, two of them even in the submicromolar range...
De novo design, synthesis, and in vitro evaluation of inhibitors for prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on binding affinityEmmanuel A Meyer
, , HCI, , Switzerland
Chembiochem 3:250-3. 2002
A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylaseU Grädler
Institut fur Pharmazeutische Chemie, Marbacher Weg 6, Philipps Universitat Marburg, 35032, Germany
J Mol Biol 306:455-67. 2001..The 1.95 A crystal structure of APH in complex with Z. mobilis TGT served as a starting point for further modification of this initial lead...
Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase to elucidate the role of serine 103 for enzymatic activityU Grädler
Institut fur Pharmazeutische Chemie, Philipps Universitat Marburg, Germany
FEBS Lett 454:142-6. 1999..The crystal structure of a TGT(S103A)/preQ1 complex combined with biochemical data presented in this paper suggest that Ser103 is essential for substrate orientation in the TGT reaction...
Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase reveal aspartate 102 as the active site nucleophileC Romier
European Molecular Biology Laboratory, Structural Biology Programme, Heidelberg, Germany
Biochemistry 35:15734-9. 1996..The mutants display only subtle changes to the wild-type protein, confirming that the observed biochemical results are due to the chemical substitutions rather than structural rearrangements...
Purification, crystallization, and preliminary x-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilisC Romier
European Molecular Biology Laboratory, Structural Biology Programme, Heidelberg, Germany
Proteins 24:516-9. 1996..1 A, b = 65.1 A, c = 71.9 A, and beta = 97.5 degrees and contain one molecule per asymmetric unit. A complete diffraction data set from one native crystal has been obtained at 1.85 A resolution...
Glutamate versus glutamine exchange swaps substrate selectivity in tRNA-guanine transglycosylase: insight into the regulation of substrate selectivity by kinetic and crystallographic studiesNaomi Tidten
Institut fur Pharmazeutische Chemie, Philipps Universitat Marburg, Marbacher Weg 6, 35032 Marburg, Germany
J Mol Biol 374:764-76. 2007..The way this is achieved, however, significantly differs from that predicted based on crystal structures of wild-type Tgt...
Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchangeC Romier
European Molecular Biology Laboratory, Structural Biology Programme, Heidelberg, Germany
EMBO J 15:2850-7. 1996..This model for tRNA binding is consistent with a base exchange mechanism involving a covalent tRNA-enzyme intermediate. This structure is the first example of a (beta/alpha)-barrel protein interacting specifically with a nucleic acid...
Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzymeK Reuter
Institut fur Biochemie, Universitat Erlangen Nurnberg, Germany
J Bacteriol 177:5284-8. 1995..mobilis Tgt was found to be a monomer according to gel filtration. In this study, it was shown that the formation of homotrimers by the E. coli enzyme is readily reversible and is dependent on protein concentration...
