Member database | CATH-Gene3D |
CATH-Gene3D type | homologous superfamily |
Description Imported from IPR027266
TrmE is a guanine nucleotide-binding protein conserved between bacteria and eukaryotes. It is involved in the modification of uridine bases at the first anticodon (wobble) position of tRNAs. The N-terminal portion of the protein is necessary for mediating dimer formation within the protein
[1].
References Imported from IPR027266
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.Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia. Lee HH, Kim DJ, Ahn HJ, Ha JY, Suh SW. J. Biol. Chem. 279, 50514-23, (2004). View articlePMID: 15355973
Further reading
3. The glycine decarboxylase system: a fascinating complex. Douce R, Bourguignon J, Neuburger M, Rebeille F. Trends Plant Sci. 6, 167-76, (2001). View articlePMID: 11286922
Integrated to
External Links
Representative structure
3tfi: DMSP-dependent demethylase from P. ubique - with substrate DMSP