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InterPro: IPR002616 Queuine/other tRNA-ribosyltransferase
Additional Reading
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Brenk R, Meyer EA, Reuter K, Stubbs MT, Garcia GA, Diederich F, Klebe G.
Crystallographic study of inhibitors of tRNA-guanine transglycosylase suggests a new structure-based pharmacophore for virtual screening.
J. Mol. Biol. 338 2004 55-75
[PubMed: 15050823]
http://dx.doi.org/10.1016/j.jmb.2004.02.019
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Tidten N, Stengl B, Heine A, Garcia GA, Klebe G, Reuter K.
Glutamate versus glutamine exchange swaps substrate selectivity in tRNA-guanine transglycosylase: insight into the regulation of substrate selectivity by kinetic and crystallographic studies.
J. Mol. Biol. 374 2007 764-76
[PubMed: 17949745]
http://dx.doi.org/10.1016/j.jmb.2007.09.062
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Stengl B, Meyer EA, Heine A, Brenk R, Diederich F, Klebe G.
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 binding.
J. Mol. Biol. 370 2007 492-511
[PubMed: 17524419]
http://dx.doi.org/10.1016/j.jmb.2007.04.008
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Hortner SR, Ritschel T, Stengl B, Kramer C, Schweizer WB, Wagner B, Kansy M, Klebe G, Diederich F.
Potent inhibitors of tRNA-guanine transglycosylase, an enzyme linked to the pathogenicity of the Shigella bacterium: charge-assisted hydrogen bonding.
Angew. Chem. Int. Ed. Engl. 46 2007 8266-9
[PubMed: 17902085]
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Ritschel T, Hoertner S, Heine A, Diederich F, Klebe G.
Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT.
Chembiochem 10 2009 716-27
[PubMed: 19199329]
http://dx.doi.org/10.1002/cbic.200800782
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InterPro 23.1
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