Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4V5Y

Crystal structure of the bacterial ribosome from Escherichia coli in complex with paromomycin and ribosome recycling factor (RRF).

This is a non-PDB format compatible entry.
Summary for 4V5Y
Entry DOI10.2210/pdb4v5y/pdb
Related2Z4L 2Z4M 2Z4N
Descriptor16S rRNA, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (57 entities in total)
Functional Keywordsrna-protein complex, ribosome
Biological sourceEscherichia coli
More
Cellular locationCytoplasm : Q9WX76
Total number of polymer chains106
Total formula weight4339771.17
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: 2007-06-19, release date: 2014-07-09, Last modification date: 2023-09-20)
Primary citationBorovinskaya, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.45 Å)
Structure validation

229183

數據於2024-12-18公開中

PDB statisticsPDBj update infoContact PDBjnumon