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記事

77 引用 (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.

元の言語英語
ページ(範囲)197-208
ページ数12
ジャーナルStructure
8
発行部数2
DOI
出版物ステータス出版済み - 2 1 2000

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Methionine-tRNA Ligase
Thermus thermophilus
Ligases
Anticodon
RNA
Transfer RNA
Arginine-tRNA Ligase
Catalytic Domain
Isoleucine-tRNA Ligase
Escherichia
Amino Acyl-tRNA Synthetases
Sequence Homology
Molecular Biology
Enzymes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

これを引用

The 2.0 Å crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. / Sugiura, Ikuko; Nureki, Osamu; Ugaji-Yoshikawa, Yoshiko; Kuwabara, Sachiko; Shimada, Atsushi; Tateno, Masaru; Lorber, Bernard; Giegé, Richard; Moras, Dino; Yokoyama, Shigeyuki; Konno, Michiko.

:: Structure, 巻 8, 番号 2, 01.02.2000, p. 197-208.

研究成果: ジャーナルへの寄稿記事

Sugiura, I, Nureki, O, Ugaji-Yoshikawa, Y, Kuwabara, S, Shimada, A, Tateno, M, Lorber, B, Giegé, R, Moras, D, Yokoyama, S & Konno, M 2000, 'The 2.0 Å crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules', Structure, 巻. 8, 番号 2, pp. 197-208. https://doi.org/10.1016/S0969-2126(00)00095-2
Sugiura, Ikuko ; Nureki, Osamu ; Ugaji-Yoshikawa, Yoshiko ; Kuwabara, Sachiko ; Shimada, Atsushi ; Tateno, Masaru ; Lorber, Bernard ; Giegé, Richard ; Moras, Dino ; Yokoyama, Shigeyuki ; Konno, Michiko. / The 2.0 Å crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. :: Structure. 2000 ; 巻 8, 番号 2. pp. 197-208.
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title = "The 2.0 {\AA} crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules",
abstract = "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 {\AA} 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.",
author = "Ikuko Sugiura and Osamu Nureki and Yoshiko Ugaji-Yoshikawa and Sachiko Kuwabara and Atsushi Shimada and Masaru Tateno and Bernard Lorber and Richard Gieg{\'e} and Dino Moras and Shigeyuki Yokoyama and Michiko Konno",
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T1 - The 2.0 Å crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules

AU - Sugiura, Ikuko

AU - Nureki, Osamu

AU - Ugaji-Yoshikawa, Yoshiko

AU - Kuwabara, Sachiko

AU - Shimada, Atsushi

AU - Tateno, Masaru

AU - Lorber, Bernard

AU - Giegé, Richard

AU - Moras, Dino

AU - Yokoyama, Shigeyuki

AU - Konno, Michiko

PY - 2000/2/1

Y1 - 2000/2/1

N2 - 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.

AB - 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.

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