Crystal structures of tyrosyl-tRNA synthetases from archaea

Mitsuo Kuratani, Hiroaki Sakai, Masahiro Takahashi, Tatsuo Yanagisawa, Takatsugu Kobayashi, Kazutaka Murayama, Lirong Chen, Zhi Jie Liu, Bi Cheng Wang, Chizu Kuroishi, Seiki Kuramitsu, Takaho Terada, Yoshitaka Bessho, Mikako Shirouzu, Shun Ichi Sekine, Shigeyuki Yokoyama

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24 Citations (Scopus)

Abstract

Tyrosyl-tRNA synthetase (TyrRS) catalyzes the tyrosylation of tRNA Tyr in a two-step reaction. TyrRS has the "HIGH" and "KMSKS" motifs, which play essential roles in the formation of the tyrosyl-adenylate from tyrosine and ATP. Here, we determined the crystal structures of Archaeoglobus fulgidus and Pyrococcus horikoshii TyrRSs in the l-tyrosine-bound form at 1.8 Å and 2.2 Å resolutions, respectively, and that of Aeropyrum pernix TyrRS in the substrate-free form at 2.2 Å. The conformation of the KMSKS motif differs among the three TyrRSs. In the A. pernix TyrRS, the KMSKS loop conformation corresponds to the ATP-bound "closed" form. In contrast, the KMSKS loop of the P. horikoshii TyrRS forms a novel 310 helix, which appears to correspond to the "semi-closed" form. This conformation enlarges the entrance to the tyrosine-binding pocket, which facilitates the pyrophosphate ion release after the tyrosyl-adenylate formation, and probably is involved in the initial tRNA binding. The KMSSS loop of the A. fulgidus TyrRS is somewhat farther from the active site and is stabilized by hydrogen bonds. Based on the three structures, possible structural changes of the KMSKS motif during the tyrosine activation reaction are discussed. We suggest that the insertion sequence just before the KMSKS motif, which exists in some archaeal species, enhances the binding affinity of the TyrRS for its cognate tRNA. In addition, a non-proline cis peptide bond, which is involved in the tRNA binding, is conserved among the archaeal TyrRSs.

Original languageEnglish
Pages (from-to)395-408
Number of pages14
JournalJournal of Molecular Biology
Volume355
Issue number3
DOIs
Publication statusPublished - 2006 Jan 20

Keywords

  • HIGH motif
  • KMSKS motif
  • Non-proline cis peptide
  • TyrAMP formation
  • Tyrosyl-tRNA synthetase (TyrRS)

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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  • Cite this

    Kuratani, M., Sakai, H., Takahashi, M., Yanagisawa, T., Kobayashi, T., Murayama, K., Chen, L., Liu, Z. J., Wang, B. C., Kuroishi, C., Kuramitsu, S., Terada, T., Bessho, Y., Shirouzu, M., Sekine, S. I., & Yokoyama, S. (2006). Crystal structures of tyrosyl-tRNA synthetases from archaea. Journal of Molecular Biology, 355(3), 395-408. https://doi.org/10.1016/j.jmb.2005.10.073