Crystal structure of the ribosome recycling factor from Escherichia coli

EMBO J. 2000 May 15;19(10):2362-70. doi: 10.1093/emboj/19.10.2362.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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

Substances

  • Bacterial Proteins
  • Proteins
  • Ribosomal Proteins
  • ribosome releasing factor