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

Summary for 2BCW

• Entry DOI: 10.2210/pdb2bcw/pdb
• Related: 1CTF 1ELO 1MMS
• Descriptor: 50S ribosomal protein L11, 50S ribosomal protein L7/L12, Elongation factor G (3 entities in total)
• Functional Keywords: components involved in interaction between ef-g and l7/l12 stalk base of the ribosome, ribosome
• Biological source: Thermotoga maritima; More
• Total number of polymer chains: 3
• Total formula weight: 20674.74

Authors

Datta, P.P.,Sharma, M.R.,Qi, L.,Frank, J.,Agrawal, R.K. (deposition date: 2005-10-19, release date: 2005-12-20, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (11.2 Å)