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-Structure paper
タイトル | Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. |
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ジャーナル・号・ページ | EMBO J, Vol. 21, Issue 13, Page 3557-3567, Year 2002 |
掲載日 | 2002年7月1日 |
著者 | Mikel Valle / Jayati Sengupta / Neil K Swami / Robert A Grassucci / Nils Burkhardt / Knud H Nierhaus / Rajendra K Agrawal / Joachim Frank / |
PubMed 要旨 | During the elongation cycle of protein biosynthesis, the specific amino acid coded for by the mRNA is delivered by a complex that is comprised of the cognate aminoacyl-tRNA, elongation factor Tu and ...During the elongation cycle of protein biosynthesis, the specific amino acid coded for by the mRNA is delivered by a complex that is comprised of the cognate aminoacyl-tRNA, elongation factor Tu and GTP. As this ternary complex binds to the ribosome, the anticodon end of the tRNA reaches the decoding center in the 30S subunit. Here we present the cryo- electron microscopy (EM) study of an Escherichia coli 70S ribosome-bound ternary complex stalled with an antibiotic, kirromycin. In the cryo-EM map the anticodon arm of the tRNA presents a new conformation that appears to facilitate the initial codon-anticodon interaction. Furthermore, the elbow region of the tRNA is seen to contact the GTPase-associated center on the 50S subunit of the ribosome, suggesting an active role of the tRNA in the transmission of the signal prompting the GTP hydrolysis upon codon recognition. |
リンク | EMBO J / PubMed:12093756 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 16.8 Å |
構造データ | EMDB-1045: Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. |
由来 |
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キーワード | TRANSLATION/RNA / EF-Tu (EF-Tu) / ternary complex / cryo-EM (低温電子顕微鏡法) / 70S E.coli ribosome / TRANSLATION-RNA COMPLEX / RNA (リボ核酸) / tRNA (転移RNA) / conformational change (コンフォメーション変化) |