PMID:10811627

Citation	Kim, KK, Min, K and Suh, SW (2000) Crystal structure of the ribosome recycling factor from Escherichia coli. EMBO J. 19:2362-70
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 alpha/beta 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.
Links	PubMed PMC384359 Online version:10.1093/emboj/19.10.2362
Keywords	Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Escherichia coli; Molecular Sequence Data; Protein Conformation; Proteins/chemistry; Proteins/genetics; Ribosomal Proteins; Ribosomes; Sequence Alignment
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