E coli tRNA coding for Glycine GCC anti-codon
E. coli tRNA-Gly (GCC) is one of four glycine tRNA isoacceptors in E. coli and carries the GCC anticodon, which decodes GGC glycine codons during translation. It is charged by glycyl-tRNA synthetase (GlyRS), one of the most structurally unusual aminoacyl-tRNA synthetases: E. coli GlyRS is an obligate (αβ)₂ heterotetramer, an "orphan" Class II aaRS whose sequence and unprecedented X-shaped architecture are distinct from all other aaRSs, including both eukaryotic and other bacterial GlyRSs. The catalytic α-subunit alone has no aminoacylation activity; both α- and β-subunits are indispensable for tRNA charging. Identity elements required for specific recognition by E. coli GlyRS are primarily located in the acceptor stem: G1:C72, C2:G71, together with the discriminator base U73 (unique to prokaryotes; eukaryotes use A73) and the anticodon bases C35 and C36. The anticodon loop is recognized by the β-subunit, while the acceptor stem is contacted by the α-subunit, representing a division of recognition labor across the heterotetramer. A co-crystal structure of EcGlyRS bound specifically to tRNA^Gly(GCC) confirms this recognition mode and reveals the largest tRNA-induced domain movement observed among any aaRS, suggesting the X-shaped architecture has evolved to accommodate the unusual spatial rearrangement required to capture its substrate.
Applications:
1) RNAcentral ID: URS00001ACE3E_511145
2) Nameki, N., Tamura, K., Asahara, H. & Hasegawa, T. (1997). Recognition of tRNA(Gly) by three widely diverged glycyl-tRNA synthetases. J. Mol. Biol. 268(3):640–647
3) Mazauric, M.H., Roy, H. & Kern, D. (1999). tRNA glycylation system from Thermus thermophilus: tRNA^Gly identity and functional interrelation with the glycylation systems from other phylae. Biochemistry 38(40):13094–13105
4) Ju, Y., Han, L., Chen, B., Luo, Z., Gu, Q., Xu, J., Yang, X.-L., Schimmel, P. & Zhou, H. (2021). X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications. Nucleic Acids Res. 49(17):10106–10119
5) Han, L., Luo, Z., Ju, Y., Chen, B., Zou, T., Wang, J., Xu, J., Gu, Q., Yang, X.-L., Schimmel, P. & Zhou, H. (2023). The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements. Science Advances 9(6) RCSB PDB: 7YSE
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