1JQT

Fitting of L11 protein in the low resolution cryo-EM map of E.coli 70S ribosome

Summary for 1JQT

• Entry DOI: 10.2210/pdb1jqt/pdb
• Related: 1EG0
• Descriptor: 50S Ribosomal protein L11 (1 entity in total)
• Functional Keywords: l11, cryo-em, 70s e.coli ribosome, ribosome
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 14865.64

Authors

Agrawal, R.K.,Linde, J.,Segupta, J.,Nierhaus, K.H.,Frank, J. (deposition date: 2001-08-07, release date: 2001-09-07, Last modification date: 2024-02-07)

Primary citation

Agrawal, R.K.,Linde, J.,Sengupta, J.,Nierhaus, K.H.,Frank, J.
Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation.
J.Mol.Biol., 311:777-787, 2001

PubMed Abstract: L11 protein is located at the base of the L7/L12 stalk of the 50 S subunit of the Escherichia coli ribosome. Because of the flexible nature of the region, recent X-ray crystallographic studies of the 50 S subunit failed to locate the N-terminal domain of the protein. We have determined the position of the complete L11 protein by comparing a three-dimensional cryo-EM reconstruction of the 70 S ribosome, isolated from a mutant lacking ribosomal protein L11, with the three-dimensional map of the wild-type ribosome. Fitting of the X-ray coordinates of L11-23 S RNA complex and EF-G into the cryo-EM maps combined with molecular modeling, reveals that, following EF-G-dependent GTP hydrolysis, domain V of EF-G intrudes into the cleft between the 23 S ribosomal RNA and the N-terminal domain of L11 (where the antibiotic thiostrepton binds), causing the N-terminal domain to move and thereby inducing the formation of the arc-like connection with the G' domain of EF-G. The results provide a new insight into the mechanism of EF-G-dependent translocation.

PubMed: 11518530
DOI: 10.1006/jmbi.2001.4907

Experimental method

ELECTRON MICROSCOPY (18 Å)