4V52

Crystal structure of the bacterial ribosome from Escherichia coli in complex with neomycin.

This is a non-PDB format compatible entry.

Summary for 4V52

• Entry DOI: 10.2210/pdb4v52/pdb
• Related: 2QAM 2QAN 2QAO
• Descriptor: 16S rRNA, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (56 entities in total)
• Functional Keywords: rna-protein complex, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 104
• Total formula weight: 4297709.09

Authors

Borovinskaya, M.A.,Pai, R.D.,Zhang, W.,Schuwirth, B.-S.,Holton, J.M.,Hirokawa, G.,Kaji, H.,Kaji, A.,Cate, J.H.D. (deposition date: 2007-06-15, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

Borovinskaya, M.A.,Pai, R.D.,Zhang, W.,Schuwirth, B.S.,Holton, J.M.,Hirokawa, G.,Kaji, H.,Kaji, A.,Cate, J.H.
Structural basis for aminoglycoside inhibition of bacterial ribosome recycling.
Nat.Struct.Mol.Biol., 14:727-732, 2007

PubMed Abstract: Aminoglycosides are widely used antibiotics that cause messenger RNA decoding errors, block mRNA and transfer RNA translocation, and inhibit ribosome recycling. Ribosome recycling follows the termination of protein synthesis and is aided by ribosome recycling factor (RRF) in bacteria. The molecular mechanism by which aminoglycosides inhibit ribosome recycling is unknown. Here we show in X-ray crystal structures of the Escherichia coli 70S ribosome that RRF binding causes RNA helix H69 of the large ribosomal subunit, which is crucial for subunit association, to swing away from the subunit interface. Aminoglycosides bind to H69 and completely restore the contacts between ribosomal subunits that are disrupted by RRF. These results provide a structural explanation for aminoglycoside inhibition of ribosome recycling.

PubMed: 17660832
DOI: 10.1038/nsmb1271

Experimental method

X-RAY DIFFRACTION (3.21 Å)