PROSITE documentation PDOC51709TrmE-type guanine nucleotide-binding (G) domain profile
The P-loop (see <PDOC00017>) guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling, and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state and an active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G) domain that is responsible for binding and hydrolysis of guanine nucleotides.
TrmE (also called MnmE) contains a canonical G domain and is conserved in all three kingdoms of life. It is involved in the modification of uridine bases (U34) at the first anticodon (wobble) position of tRNAs decoding two-family box triplets. TrmE is organized as a multidomain protein consisting of an ~220-amino acid N-terminal domain, probably required for self-assembly, a middle GTPase domain, of about 160 residues, and an ~75-amino acid C-terminal domain, which contains a highly conserved CxGK motif. TrmE contains at least four of the five conserved nucleotide-binding motifs G1 (GxxxxGK[ST] or P-loop), G2 (T), G3 (DxxG) and G4 ([NT]KxD). The totally invariant alanine in the SA[KL] (G5) motif of Ras anGalph proteins is less well conserved [1,2,3,4,5].
The structure of the TrmE-type G domain consists of a central four-stranded β-sheet flanked by five α-helices (see <PDB:1XZP>). It dimerises in a potassium-dependent manner [4,5].
The profile we developed covers the entire TmrE-type G domain.
Last update:March 2014 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Leipe D.D. Wolf Y.I. Koonin E.V. Aravind L. |
| Title | Classification and evolution of P-loop GTPases and related ATPases. | |
| Source | J. Mol. Biol. 317:41-72(2002). | |
| PubMed ID | 11916378 | |
| DOI | 10.1006/jmbi.2001.5378 |
| 2 | Authors | Yamanaka K. Hwang J. Inouye M. |
| Title | Characterization of GTPase activity of TrmE, a member of a novel GTPase superfamily, from Thermotoga maritima. | |
| Source | J. Bacteriol. 182:7078-7082(2000). | |
| PubMed ID | 11092873 |
| 3 | Authors | Yim L. Martinez-Vicente M. Villarroya M. Aguado C. Knecht E. |
| Title | Armengod M.-E. The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function. | |
| Source | J. Biol. Chem. 278:28378-28387(2003). | |
| PubMed ID | 12730230 | |
| DOI | 10.1074/jbc.M301381200 |
| 4 | Authors | Scrima A. Vetter I.R. Armengod M.E. Wittinghofer A. |
| Title | The structure of the TrmE GTP-binding protein and its implications for tRNA modification. | |
| Source | EMBO J. 24:23-33(2005). | |
| PubMed ID | 15616586 | |
| DOI | 10.1038/sj.emboj.7600507 |
| 5 | Authors | Monleon D. Martinez-Vicente M. Esteve V. Yim L. Prado S. Armengod M.-E. Celda B. |
| Title | Structural insights into the GTPase domain of Escherichia coli MnmE protein. | |
| Source | Proteins 66:726-739(2007). | |
| PubMed ID | 17143896 | |
| DOI | 10.1002/prot.21186 |
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