4V57

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

Summary for 4V57

Entry DOI	10.2210/pdb4v57/pdb
Related	2QOZ 2QP0 2QP1
Descriptor	16S rRNA, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (57 entities in total)
Functional Keywords	rna-protein complex, ribosome
Biological source	Escherichia coli More
Total number of polymer chains	104
Total formula weight	4298300.88
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.5 Å)

Structure validation