Article
- The EMBO Journal (2000) 19, 2362 - 2370
- doi:10.1093/emboj/19.10.2362
Crystal structure of the ribosome recycling factor from Escherichia coli
Kyeong Kyu Kim1, Kyeongsik Min1 and Se Won Suh2
- Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Chinju 660-701, Korea
- Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea
Correspondence to:
Kyeong Kyu Kim, E-mail: kim@px1.gsnu.ac.kr
Received 29 October 1999; Accepted 20 March 2000; Revised 20 March 2000
Abstract
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 
/
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.
Keywords:
- crystal structure,
- protein synthesis,
- ribosome recycling factor,
- translation,
- tRNA
