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-Structure paper
タイトル | High resolution structure of the large ribosomal subunit from a mesophilic eubacterium. |
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ジャーナル・号・ページ | Cell, Vol. 107, Issue 5, Page 679-688, Year 2001 |
掲載日 | 2001年11月30日 |
著者 | J Harms / F Schluenzen / R Zarivach / A Bashan / S Gat / I Agmon / H Bartels / F Franceschi / A Yonath / |
PubMed 要旨 | We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ...We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The over-all structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit of tRNA. |
リンク | Cell / PubMed:11733066 |
手法 | X線回折 |
解像度 | 3.1 Å |
構造データ | PDB-1nkw: |
由来 |
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キーワード | RIBOSOME / Ribosome; large subunit; 50S; Deinococcus Radiodurans; X-ray structure; peptidyl-transferase / peptide bond formation |