Member database | NCBIfam (includes TIGRFAMs) |
NCBIfam type | family |
Short name | leuS_bact |
Description
The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches.
References
1. Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination. Liu Y, Liao J, Zhu B, Wang ED, Ding J. Biochem. J. 394, 399-407, (2006). View articlePMID: 16277600
2. Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator-base recognition. Fukunaga R, Yokoyama S. Nat Struct Mol Biol 12, 915-22, (2005). PMID: 16155584
3. Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution. Zhao MW, Zhu B, Hao R, Xu MG, Eriani G, Wang ED. EMBO J 24, 1430-9, (2005). PMID: 15775966