title: Crystal structure of the ribosome recycling factor from Escherichia coli.
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.
authors.affiliation: Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Chinju 660-701, Korea. kim@px1.gsnu.ac.kr
authors.forename: K K
authors.initials: KK
authors.lastname: Kim
authors.forename: K
authors.initials: K
authors.lastname: Min
authors.forename: S W
authors.initials: SW
authors.lastname: Suh
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D012269:Ribosomal Proteins; D012270:Ribosomes; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D011506:Proteins; D012269:Ribosomal Proteins; C087267:ribosome releasing factor