2BCW

Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of ribosomal protein L7/L12 and a portion of the G' domain of elongation factor G, as fitted into cryo-em map of an Escherichia coli 70S*EF-G*GDP*fusidic acid complex

2BCW の概要

• エントリーDOI: 10.2210/pdb2bcw/pdb
• 関連するPDBエントリー: 1CTF 1ELO 1MMS
• 分子名称: 50S ribosomal protein L11, 50S ribosomal protein L7/L12, Elongation factor G (3 entities in total)
• 機能のキーワード: components involved in interaction between ef-g and l7/l12 stalk base of the ribosome, ribosome
• 由来する生物種: Thermotoga maritima; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 20674.74

構造登録者

Datta, P.P.,Sharma, M.R.,Qi, L.,Frank, J.,Agrawal, R.K. (登録日: 2005-10-19, 公開日: 2005-12-20, 最終更新日: 2024-02-14)

主引用文献

Datta, P.P.,Sharma, M.R.,Qi, L.,Frank, J.,Agrawal, R.K.
Interaction of the G' Domain of Elongation Factor G and the C-Terminal Domain of Ribosomal Protein L7/L12 during Translocation as Revealed by Cryo-EM.
Mol.Cell, 20:723-731, 2005

PubMed Abstract: During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state. To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with three-dimensional cryo-electron microscopy (cryo-EM). Two distinct positions for the undecagold, observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labeled amino acid. Molecular analyses of the cryo-EM maps show: (1) that three structural components, the N-terminal domain of ribosomal protein L11, the C-terminal domain of ribosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conformational changes to form the ALC.

PubMed: 16337596
DOI: 10.1016/j.molcel.2005.10.028

実験手法

ELECTRON MICROSCOPY (11.2 Å)