Structures of the bacterial ribosome at 3.5 A resolution

Science. 2005 Nov 4;310(5749):827-34. doi: 10.1126/science.1117230.

Abstract

We describe two structures of the intact bacterial ribosome from Escherichia coli determined to a resolution of 3.5 angstroms by x-ray crystallography. These structures provide a detailed view of the interface between the small and large ribosomal subunits and the conformation of the peptidyl transferase center in the context of the intact ribosome. Differences between the two ribosomes reveal a high degree of flexibility between the head and the rest of the small subunit. Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA (mRNA) and transfer RNAs (tRNAs) during translocation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / chemistry*
  • Escherichia coli / ultrastructure*
  • Escherichia coli Proteins / biosynthesis
  • Escherichia coli Proteins / chemistry
  • Hydrogen Bonding
  • Magnesium / metabolism
  • Models, Molecular
  • Nucleic Acid Conformation
  • Peptidyl Transferases / chemistry
  • Protein Biosynthesis
  • Protein Conformation
  • RNA, Bacterial / chemistry
  • RNA, Bacterial / metabolism
  • RNA, Messenger / chemistry
  • RNA, Messenger / metabolism
  • RNA, Ribosomal / chemistry*
  • RNA, Transfer / chemistry
  • RNA, Transfer / metabolism
  • Ribosomal Proteins / chemistry*
  • Ribosomes / chemistry*
  • Ribosomes / ultrastructure*

Substances

  • Escherichia coli Proteins
  • RNA, Bacterial
  • RNA, Messenger
  • RNA, Ribosomal
  • Ribosomal Proteins
  • RNA, Transfer
  • Peptidyl Transferases
  • Magnesium

Associated data

  • PDB/2AVY
  • PDB/2AW4
  • PDB/2AW7
  • PDB/2AWB