4W2E

Crystal structure of Elongation Factor 4 (EF4/LepA) bound to the Thermus thermophilus 70S ribosome

これはPDB形式変換不可エントリーです。

4W2E の概要

• エントリーDOI: 10.2210/pdb4w2e/pdb
• 分子名称: 23S Ribosomal RNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (62 entities in total)
• 機能のキーワード: ef4, lepa, translation, elogation, acylated p-site trna, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 57
• 化学式量合計: 2339375.44

構造登録者

Gagnon, M.G.,Lin, J.,Steitz, T.A. (登録日: 2014-06-04, 公開日: 2014-10-01, 最終更新日: 2024-11-06)

主引用文献

Gagnon, M.G.,Lin, J.,Bulkley, D.,Steitz, T.A.
Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome.
Science, 345:684-687, 2014

PubMed Abstract: Elongation factor 4 (EF4/LepA) is a highly conserved guanosine triphosphatase translation factor. It was shown to promote back-translocation of tRNAs on posttranslocational ribosome complexes and to compete with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis. Here, we report a crystal structure of EF4-guanosine diphosphate bound to the Thermus thermophilus ribosome with a P-site tRNA at 2.9 angstroms resolution. The C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the acceptor stem of the peptidyl-tRNA in the P site. The ribosome is in an unusual state of ratcheting with the 30S subunit rotated clockwise relative to the 50S subunit, resulting in a remodeled decoding center. The structure is consistent with EF4 functioning either as a back-translocase or a ribosome sequester.

PubMed: 25104389
DOI: 10.1126/science.1253525

実験手法

X-RAY DIFFRACTION (2.9 Å)