1a8h
From Proteopedia
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'''METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS''' | '''METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS''' | ||
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[[Category: Ugaji, Y.]] | [[Category: Ugaji, Y.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: Aminoacyl-trna synthetase]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rossmann fold]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:58, 2 May 2008
METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
Overview
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 A 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 coli MetRS. The conserved 'anticodon-binding' residues are spatially clustered on an alpha-helix-bundle domain. The Rossmann-fold and anticodon-binding domains are connected by a beta-alpha-alpha-beta-alpha topology ('SC fold') domain that contains the class I specific KMSKS motif. Conclusions: The alpha-helix-bundle domain identified in the MetRS structure is the signature of the class Ia enzymes, as it was also identified in the class Ia structures of the isoleucyl- and arginyl-tRNA synthetases. The beta-alpha-alpha-beta-alpha 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.
About this Structure
1A8H is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules., Sugiura I, Nureki O, Ugaji-Yoshikawa Y, Kuwabara S, Shimada A, Tateno M, Lorber B, Giege R, Moras D, Yokoyama S, Konno M, Structure. 2000 Feb 15;8(2):197-208. PMID:10673435 Page seeded by OCA on Fri May 2 09:58:12 2008
Categories: Methionine--tRNA ligase | Single protein | Thermus thermophilus | Giege, R. | Konno, M. | Kuwabara, S. | Lober, B. | Moras, D. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sugiura, I. | Ugaji, Y. | Yokoyama, S. | Aminoacyl-trna synthetase | Riken structural genomics/proteomics initiative | Rossmann fold | Rsgi | Structural genomic
