A steric block in translation caused by the antibiotic spectinomycin

被引：112

作者：

Borovinskaya, Maria A.

Shoji, Shinichiro

Holton, James M.

Fredric, Kurt

Cate, Jamie H. D. ^{[1
]}

机构：

[1] Lawrence Berkeley Natl Lab, Phys Biosci Div, Berkeley, CA 94720 USA

[2] Ohio State Univ, Dept Microbiol, Columbus, OH 43210 USA

[3] Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA

[4] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94158 USA

[5] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[6] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

来源：

ACS CHEMICAL BIOLOGY | 2007年 / 2卷 / 08期

关键词：

D O I：

10.1021/cb700100n

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

收藏

页码：545 / 552

页数：8

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