E coli tRNA coding for tryptophan CCA anti-codon
E. coli tRNA-Trp (CCA) is the sole tRNA responsible for decoding UGG tryptophan codons during translation. It is charged by tryptophanyl-tRNA synthetase (TrpRS), a Class I homodimeric aminoacyl-tRNA synthetase that exhibits half-of-the-sites reactivity, meaning only one of its two active sites is occupied by the reaction intermediate at a given time. The primary identity elements for TrpRS recognition are the discriminator base G73, which is conserved across prokaryotic tRNA-Trp sequences and whose substitution severely impairs aminoacylation, and all three bases of the CCA anticodon, each of which is individually required for tryptophan insertion in vivo. The A1–U72 base pair at the first position of the acceptor stem is a weak secondary recognition element. Unlike its eukaryotic counterpart, bacterial TrpRS relies on an asymmetric "open-closed" conformation to functionally engage tRNA-Trp, a structural feature absent in human TrpRS and of significant interest for selective antibacterial discovery.
Applications:
1) RNAcentral ID: URS00003A6DC6_511145
2) Himeno, H., Hasegawa, T., Asahara, H., Tamura, K. & Shimizu, M. (1991). Identity determinants of E. coli tryptophan tRNA. Nucleic Acids Res. 19(23):6379–6382
3) Pak, M., Pallanck, L. & Schulman, L.H. (1992). Conversion of a methionine initiator tRNA into a tryptophan-inserting elongator tRNA in vivo. Biochemistry 31(13):3303–3309
4) Xiang, M., Xia, K., Chen, B., Luo, Z., Yu, Y., Jiang, L. & Zhou, H. (2023). An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening. Nucleic Acids Res. 51(9):4637–4649 RCSB PDB: 8I4I
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