3DEG

Complex of elongating Escherichia coli 70S ribosome and EF4(LepA)-GMPPNP

3DEG の概要

• エントリーDOI: 10.2210/pdb3deg/pdb
• EMDBエントリー: 1524
• 分子名称: A/L-tRNA, 30S ribosomal protein S12, 50S ribosomal protein L11, ... (11 entities in total)
• 機能のキーワード: ribosome, translation, lepa, ef4, gtp-binding, membrane, nucleotide-binding, antibiotic resistance, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, methylation
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 190058.63

構造登録者

Connell, S.R.,Topf, M.,Qin, Y.,Wilson, D.N.,Mielke, T.,Fucini, P.,Nierhaus, K.H.,Spahn, C.M.T. (登録日: 2008-06-10, 公開日: 2008-08-19, 最終更新日: 2024-03-20)

主引用文献

Connell, S.R.,Topf, M.,Qin, Y.,Wilson, D.N.,Mielke, T.,Fucini, P.,Nierhaus, K.H.,Spahn, C.M.T.
A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation
Nat.Struct.Mol.Biol., 15:910-915, 2008

PubMed Abstract: EF4 (LepA) is an almost universally conserved translational GTPase in eubacteria. It seems to be essential under environmental stress conditions and has previously been shown to back-translocate the tRNAs on the ribosome, thereby reverting the canonical translocation reaction. In the current work, EF4 was directly visualized in the process of back-translocating tRNAs by single-particle cryo-EM. Using flexible fitting methods, we built a model of ribosome-bound EF4 based on the cryo-EM map and a recently published unbound EF4 X-ray structure. The cryo-EM map establishes EF4 as a noncanonical elongation factor that interacts not only with the elongating ribosome, but also with the back-translocated tRNA in the A-site region, which is present in a previously unseen, intermediate state and deviates markedly from the position of a canonical A-tRNA. Our results, therefore, provide insight into the underlying structural principles governing back-translocation.

PubMed: 19172743
DOI: 10.1038/nsmb.1469

実験手法

ELECTRON MICROSCOPY (10.9 Å)