4V56

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

This is a non-PDB format compatible entry.

Summary for 4V56

• Entry DOI: 10.2210/pdb4v56/pdb
• Related: 2QOV 2QOW 2QOX
• Descriptor: 16S rRNA, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (56 entities in total)
• Functional Keywords: rna-protein complex, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, antibiotic resistance, repressor, transcription, transcription regulation, transcription termination, translation regulation, acetylation, trna-binding, methylation, endonuclease, hydrolase, nuclease, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 104
• Total formula weight: 4295842.30

Authors

Borovinskaya, M.A.,Shoji, S.,Holton, J.M.,Fredrick, K.,Cate, J.H.D. (deposition date: 2007-07-21, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

Borovinskaya, M.A.,Shoji, S.,Holton, J.M.,Fredrick, K.,Cate, J.H.
A steric block in translation caused by the antibiotic spectinomycin.
Acs Chem.Biol., 2:545-552, 2007

PubMed Abstract: The widely used antibiotic spectinomycin inhibits bacterial protein synthesis by blocking translocation of messenger RNA and transfer RNAs on the ribosome. Here, we show that in crystals of the Escherichia coli 70S ribosome spectinomycin binding traps a distinct swiveling state of the head domain of the small ribosomal subunit. Spectinomycin also alters the rate and completeness of reverse translocation in vitro. These structural and biochemical data indicate that in solution spectinomycin sterically blocks swiveling of the head domain of the small ribosomal subunit and thereby disrupts the translocation cycle.

PubMed: 17696316
DOI: 10.1021/cb700100n

Experimental method

X-RAY DIFFRACTION (3.93 Å)