Crystal structure of the ribosome recycling factor from Escherichia coli

被引:79
作者
Kim, KK [1 ]
Min, K
Suh, SW
机构
[1] Gyeongsang Natl Univ, Plant Mol Biol & Biotechnol Res Ctr, Chinju 660701, South Korea
[2] Seoul Natl Univ, Coll Nat Sci, Dept Chem, Seoul 151742, South Korea
关键词
crystal structure; protein synthesis; ribosome recycling factor; translation; tRNA;
D O I
10.1093/emboj/19.10.2362
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
We have determined the crystal structure of the Escherichia coli ribosome recycling factor (RRF), which catalyzes the disassembly of the termination complex in protein synthesis. The L-shaped molecule consists of two domains: a triple-stranded antiparallel coiled-coil and an alp domain. The coil domain has a cylindrical shape and negatively charged surface, which are reminiscent of the anticodon arm of tRNA and domain IV of elongation factor EF-G. We suggest that RRF binds to the ribosomal A-site through its coil domain, which is a tRNA mimic. The relative position of the two domains is changed about an axis along the hydrophobic cleft in the hinge where the alkyl chain of a detergent molecule is bound. The tRNA mimicry and the domain movement observed in RRF provide a structural basis for understanding the role of RRF in protein synthesis.
引用
收藏
页码:2362 / 2370
页数:9
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