The ribosome-structure and functional ligand-binding experiments using cryo-electron microscopy

J Struct Biol. 1998 Dec 15;124(2-3):142-50. doi: 10.1006/jsbi.1998.4071.

Abstract

Cryo-electron microscopy has greatly advanced our understanding of the basic steps of protein synthesis in the bacterial ribosome. This article gives an overview of what has been achieved so far. Through three-dimensional visualization of complexes that represent the ribosome in defined binding states, locations were derived for the tRNA in A, P, and E sites, as well as the elongation factors. In addition, the pathways of messenger RNA and the exiting polypeptide chain could be inferred.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / metabolism
  • Bacterial Proteins / ultrastructure
  • Binding Sites
  • Cryoelectron Microscopy / methods
  • Escherichia coli / metabolism
  • Escherichia coli / ultrastructure
  • Ligands
  • Models, Structural
  • RNA, Bacterial / metabolism
  • RNA, Bacterial / ultrastructure
  • RNA, Ribosomal / metabolism
  • RNA, Ribosomal / ultrastructure
  • Ribosomal Proteins / metabolism
  • Ribosomal Proteins / ultrastructure
  • Ribosomes / metabolism*
  • Ribosomes / ultrastructure*

Substances

  • Bacterial Proteins
  • Ligands
  • RNA, Bacterial
  • RNA, Ribosomal
  • Ribosomal Proteins