The 2.0 Å crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules

Ikuko Sugiura, Osamu Nureki, Yoshiko Ugaji-Yoshikawa, Sachiko Kuwabara, Atsushi Shimada, Masaru Tateno, Bernard Lorber, Richard Giegé, Dino Moras, Shigeyuki Yokoyama, Michiko Konno

研究成果: ジャーナルへの寄稿学術誌査読

82 被引用数 (Scopus)

抄録

Background: The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold, which is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses, a, b and c, according to sequence homology. No conserved structural features for tRNA recognition by class I synthetases have been established. Results: We determined the crystal structure of the class Ia methionyl-tRNA synthetase (MetRS) at 2.0 Å resolution, using MetRS from an extreme thermophile, Thermus thermophilus HB8. The T. thermophilus MetRS structure is in full agreement with the biochemical and genetic data from Escherichia coil MetRS. The conserved 'anticodon-binding' residues are spatially clustered on an α-helix-bundle domain. The Rossmann-fold and anticodon-binding domains are connected by a β-α-α-β-α topology ('SC fold') domain that contains the class I specific KMSKS motif. Conclusions: The α-helix-bundle domain identified in the MetRS structure is the signature of the class la enzymes, as it was also identified in the class la structures of the isoleucyl- and arginyl-tRNA synthetases. The β-α-α-β-α topology domain, which can now be identified in all known structures of the class Ia and Ib synthetases, is likely to dock with the inner side of the L-shaped tRNA, thereby positioning the anticodon stem.

本文言語英語
ページ(範囲)197-208
ページ数12
ジャーナルStructure
8
2
DOI
出版ステータス出版済み - 2月 1 2000
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 分子生物学

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