TRNA-guanine transglycosylase

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Structure of tRNA-guanine transglycosylase complex with queuine precursor and Zn+2 ion (grey) (PDB entry 1p0e)

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Updated on 26-October-2017

↑ Nonekowski ST, Garcia GA. tRNA recognition by tRNA-guanine transglycosylase from Escherichia coli: the role of U33 in U-G-U sequence recognition. RNA. 2001 Oct;7(10):1432-41. PMID:11680848
↑ Sabina J, Soll D. The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosine formation. J Biol Chem. 2006 Mar 17;281(11):6993-7001. Epub 2006 Jan 10. PMID:16407303 doi:http://dx.doi.org/M512841200
↑ Brenk R, Stubbs MT, Heine A, Reuter K, Klebe G. 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. Chembiochem. 2003 Oct 6;4(10):1066-77. PMID:14523925 doi:10.1002/cbic.200300644

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-	<StructureSection load='' size='400' side='right' caption='Structure of tRNA-guanine transglycosylase complex with queuine precursor (PDB entry [[1p0e]])' scene='55/551184/Cv/1'>	+	<StructureSection load='' size='400' side='right' caption='Structure of tRNA-guanine transglycosylase complex with queuine precursor and Zn+2 ion (grey) (PDB entry [[1p0e]])' scene='55/551184/Cv/1'>

	'''tRNA-guanine transglycosylase''' (TGT) is involved in the post-transcriptional modification of tRNA. TGT is involved in the replacement of guanine-34 by queuine precursor (preQ1) in the anticodon of tRNA<ref>PMID:11680848</ref>. In archaebacteria TGT (ATGT) catalyzes the introduction of archaeosin precursor (preQ0) into the D-loop of tRNA<ref>PMID:16407303</ref>.		'''tRNA-guanine transglycosylase''' (TGT) is involved in the post-transcriptional modification of tRNA. TGT is involved in the replacement of guanine-34 by queuine precursor (preQ1) in the anticodon of tRNA<ref>PMID:11680848</ref>. In archaebacteria TGT (ATGT) catalyzes the introduction of archaeosin precursor (preQ0) into the D-loop of tRNA<ref>PMID:16407303</ref>.