期刊
ACS CHEMICAL BIOLOGY
卷 2, 期 8, 页码 545-552出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb700100n
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资金
- NCI NIH HHS [CA92584, P01 CA092584] Funding Source: Medline
- NIGMS NIH HHS [R01 GM072528, R01 GM065050, GM65050, R01 GM072528-04, GM072528] Funding Source: Medline
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.
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