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InterPro: IPR002616 Queuine/other tRNA-ribosyltransferase

Protein matchesHelp
UniProtKB
Matches:
2109 proteins
AccessionHelp IPR002616 tRNA_ribo_trans
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004803 Queuine tRNA-ribosyltransferase
IPR004804 Archaeosine tRNA-ribosyltransferase
GO Term annotationHelp
Process GO:0006400 tRNA modification
GO:0008616 queuosine biosynthetic process
Function GO:0008479 queuine tRNA-ribosyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This is a family of queuine, archaeosine and general tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine at position 34 and with archaeosine at position 15 in archaeal tRNAs. In bacterial it catalyses the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position [1, 2]. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues [1].

Structural linksHelp
PDB - click here
SCOP: c.1.20.1 , d.17.6.1
Database linksHelp
Enzyme: EC:2.4.2.29
PANDIT: PF01702
Blocks: IPB002616

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002616 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
B8ZXI1 Queuine tRNA-ribosyltransferase subunit QTRTD1

Q23623 Probable queuine tRNA-ribosyltransferase

Q55983 Queuine tRNA-ribosyltransferase

Q9BXR0 Queuine tRNA-ribosyltransferase

Q9VPY8 Probable queuine tRNA-ribosyltransferase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR004803 Queuine tRNA-ribosyltransferase
IPR002616 Queuine/other tRNA-ribosyltransferase
SWISS-MODEL
ModBase

PublicationsHelp
1. Romier C, Reuter K, Suck D, Ficner R.
Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange.
EMBO J. 15 2850-7 1996 [PubMed: 8654383]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8654383
2. Garcia GA, Koch KA, Chong S.
tRNA-guanine transglycosylase from Escherichia coli. Overexpression, purification and quaternary structure.
J. Mol. Biol. 231 489-97 1993 [PubMed: 8323579]
http://dx.doi.org/10.1006/jmbi.1993.1296

Additional ReadingHelp
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
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
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
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]
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