TRNA-guanine transglycosylase

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tRNA-guanine transglycosylase (TGT) or queuine tRNA-ribosyltransferase 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[1]. In archaebacteria TGT (ATGT) catalyzes the introduction of archaeosin precursor (preQ0) into the D-loop of tRNA[2].

Structural highlights

TGT overall structure is of a Tim barrel. A structural Zn+2 ion is tetrahedrally coordinated in the C-terminal subdomain. The active site contains queuine precursor[3].

3D structures of tRNA-guanine transglycosylase

tRNA-guanine transglycosylase 3D structures


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

Drag the structure with the mouse to rotate

References

  1. 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
  2. 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
  3. 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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