IPR018948
GTP-binding protein TrmE, N-terminal
InterPro entry
Short name | GTP-bd_TrmE_N |
Overlapping homologous superfamilies |
Description
This entry represents the N-terminal domain of tRNA modification GTPase MnmE (also known as TrmE) and similar proteins found in bacteria and eukaryotes. MnmE is a guanine nucleotide-binding protein involved in the modification of the wobble position of certain tRNAs that binds and hydrolyses GTP. TrmE actively participates in the formylation reaction of uridine and regulates the ensuing hydrogenation reaction of a Schiff's base intermediate. This domain consists of five β-strands and three α-helices and is necessary for mediating dimer formation within the protein. It is homologous to the tetrahydrofolate-binding domain of N,N-dimethylglycine oxidase and indeed binds formyl-tetrahydrofolate
[1, 2].
References
1.The structure of the TrmE GTP-binding protein and its implications for tRNA modification. Scrima A, Vetter IR, Armengod ME, Wittinghofer A. EMBO J. 24, 23-33, (2005). View articlePMID: 15616586
2.Kissing G domains of MnmE monitored by X-ray crystallography and pulse electron paramagnetic resonance spectroscopy. Meyer S, Bohme S, Kruger A, Steinhoff HJ, Klare JP, Wittinghofer A. PLoS Biol. 7, e1000212, (2009). View articlePMID: 19806182
Cross References
ENZYME