4V6A

Structure of EF-P bound to the 70S ribosome.

これはPDB形式変換不可エントリーです。

4V6A の概要

• エントリーDOI: 10.2210/pdb4v6a/pdb
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total)
• 機能のキーワード: translation, elongation factor, initiation, l1-stalk, ribosome
• 由来する生物種: Thermus thermophilus HB8; 詳細
• 細胞内の位置: Cytoplasm : Q76G20
• タンパク質・核酸の鎖数: 112
• 化学式量合計: 4498367.14

構造登録者

Stanley, R.E.,Blaha, G. (登録日: 2009-06-15, 公開日: 2014-07-09, 最終更新日: 2023-09-20)

主引用文献

Blaha, G.,Stanley, R.E.,Steitz, T.A.
Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome.
Science, 325:966-970, 2009

PubMed Abstract: Elongation factor P (EF-P) is an essential protein that stimulates the formation of the first peptide bond in protein synthesis. Here we report the crystal structure of EF-P bound to the Thermus thermophilus 70S ribosome along with the initiator transfer RNA N-formyl-methionyl-tRNA(i) (fMet-tRNA(i)(fMet)) and a short piece of messenger RNA (mRNA) at a resolution of 3.5 angstroms. EF-P binds to a site located between the binding site for the peptidyl tRNA (P site) and the exiting tRNA (E site). It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. Domain II of EF-P interacts with the ribosomal protein L1, which results in the largest movement of the L1 stalk that has been observed in the absence of ratcheting of the ribosomal subunits. EF-P facilitates the proper positioning of the fMet-tRNA(i)(fMet) for the formation of the first peptide bond during translation initiation.

PubMed: 19696344
DOI: 10.1126/science.1175800

実験手法

X-RAY DIFFRACTION (3.1 Å)