5LZC
Structure of SelB-Sec-tRNASec bound to the 70S ribosome in the codon reading state (CR)
これはPDB形式変換不可エントリーです。
5LZC の概要
エントリーDOI | 10.2210/pdb5lzc/pdb |
EMDBエントリー | 4123 |
分子名称 | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (64 entities in total) |
機能のキーワード | translation, decoding, recoding, selenocysteine, ribosome |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 58 |
化学式量合計 | 2268822.70 |
構造登録者 | Fischer, N.,Neumann, P.,Bock, L.V.,Maracci, C.,Wang, Z.,Paleskava, A.,Konevega, A.L.,Schroeder, G.F.,Grubmueller, H.,Ficner, R.,Rodnina, M.V.,Stark, H. (登録日: 2016-09-29, 公開日: 2016-11-23, 最終更新日: 2024-10-23) |
主引用文献 | Fischer, N.,Neumann, P.,Bock, L.V.,Maracci, C.,Wang, Z.,Paleskava, A.,Konevega, A.L.,Schroder, G.F.,Grubmuller, H.,Ficner, R.,Rodnina, M.V.,Stark, H. The pathway to GTPase activation of elongation factor SelB on the ribosome. Nature, 540:80-85, 2016 Cited by PubMed Abstract: In all domains of life, selenocysteine (Sec) is delivered to the ribosome by selenocysteine-specific tRNA (tRNA) with the help of a specialized translation factor, SelB in bacteria. Sec-tRNA recodes a UGA stop codon next to a downstream mRNA stem-loop. Here we present the structures of six intermediates on the pathway of UGA recoding in Escherichia coli by single-particle cryo-electron microscopy. The structures explain the specificity of Sec-tRNA binding by SelB and show large-scale rearrangements of Sec-tRNA. Upon initial binding of SelB-Sec-tRNA to the ribosome and codon reading, the 30S subunit adopts an open conformation with Sec-tRNA covering the sarcin-ricin loop (SRL) on the 50S subunit. Subsequent codon recognition results in a local closure of the decoding site, which moves Sec-tRNA away from the SRL and triggers a global closure of the 30S subunit shoulder domain. As a consequence, SelB docks on the SRL, activating the GTPase of SelB. These results reveal how codon recognition triggers GTPase activation in translational GTPases. PubMed: 27842381DOI: 10.1038/nature20560 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (4.8 Å) |
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