Protein Family Models

This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme. [1]. 11224561. Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase. Sekine S, Nureki O, Shimada A, Vassylyev DG, Yokoyama S;. Nat Struct Biol. 2001;8:203-206. [2]. 7701318. Architectures of class-defining and specific domains of glutamyl-tRNA synthetase. Nureki O, Vassylyev DG, Katayanagi K, Shimizu T, Sekine S, Kigawa T, Miyazawa T, Yokoyama S, Morikawa K;. Science. 1995;267:1958-1965. [3]. 12554668. ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. Sekine S, Nureki O, Dubois DY, Bernier S, Chenevert R, Lapointe J, Vassylyev DG, Yokoyama S;. EMBO J. 2003;22:676-688. [4]. 20606262. Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima. Ito T, Kiyasu N, Matsunaga R, Takahashi S, Yokoyama S;. Acta Crystallogr D Biol Crystallogr. 2010;66:813-820. [5]. 20882017. Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions. Ito T, Yokoyama S;. Nature. 2010;467:612-616. [6]. 28303005. Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms. Moen SO, Edwards TE, Dranow DM, Clifton MC, Sankaran B, Van Voorhis WC, Sharma A, Manoil C, Staker BL, Myler PJ, Lorimer DD;. Sci Rep. 2017;7:223. (from Pfam)

Date:

2024-10-16

Members of this family include glutamate--tRNA ligases and tRNA glutamyl-Q(34) synthetase, both of which bind a tRNA and attach a glutamate residue, although at different sites on tRNA molecules, the latter at the anticodon site. It would be misleading to call the latter a glutamate--tRNA ligase, as the reaction is for base modification, rather than charging the tRNA with an amino acid destined for use in translation.

Date:

2024-10-16

glutamate--tRNA ligase catalyzes the attachment of glutamate to tRNA(Glu)

Date:

2017-02-22

The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This HMM models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences.

Gene:

gltX

Date:

2024-05-15