E coli tRNA coding for Aspartate GTC anti-codon
E. coli tRNA^Asp(GTC) is a 77-nucleotide transfer RNA that decodes GAC and GAU aspartate codons via its GTC (GUC) anticodon and is aminoacylated by aspartyl-tRNA synthetase (AspRS), a class IIb enzyme. It adopts the canonical cloverleaf secondary structure and L-shaped tertiary fold, with a short variable loop characteristic of class I tRNAs. The anticodon loop harbors a queuosine (Q) modification at the wobble position 34 in vivo, which enhances decoding fidelity at the ribosomal A-site. While there are no modified bases in this tRNA, it is still a valuable tool for in vitro studies. The GTC anticodon and discriminator base G73 together constitute the primary identity elements for AspRS recognition. Crystal structure analysis of the unmodified form (PDB: 6UGG) revealed that tRNA^Asp exhibits intrinsic structural flexibility and plasticity even in the absence of protein partners, with two closely related conformations observed within the same crystal, demonstrating that tRNA structural dynamics are an inherent property of the molecule rather than being solely induced by synthetase or ribosome binding. Its well-characterized structure and aminoacylation identity rules have made it a central model system in tRNA biology and synthetase specificity research.
Applications -
1) RNAcentral ID: URS000009EE82_511145
2) Perret, V., et al. (1990). "Conformation in solution of yeast tRNA^Asp molecules with an unmodified anticodon loop." Biochimie, 72(10), 735–743
3) Chan, C. W., Badong, D., Rajan, R., & Mondragón, A. (2019). "Crystal structures of an unmodified bacterial tRNA reveal intrinsic structural flexibility and plasticity as general properties of unbound tRNAs." RNA, 26(3), 278–289 PDB ID: 6UGG
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