Structural basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex.

@article{Numata2006StructuralBF,
  title={Structural basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex.},
  author={Tomoyuki Numata and Shuya Fukai and Yoshiho Ikeuchi and Tsutomu Suzuki and Osamu Nureki},
  journal={Structure},
  year={2006},
  volume={14 2},
  pages={357-66}
}
Uridine at wobble position 34 of tRNA(Lys), tRNA(Glu), and tRNA(Gln) is exclusively modified into 2-thiouridine (s2U), which is crucial for both precise codon recognition and recognition by the cognate aminoacyl-tRNA synthetases. Recent Escherichia coli genetic studies revealed that the products of five novel genes, tusABCDE, function in the s2U modification. Here, we solved the 2.15 angstroms crystal structure of the E. coli TusBCD complex, a sulfur transfer mediator, forming a heterohexamer… CONTINUE READING

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