Structure of the 70S ribosome complexed with mRNA and tRNA

Science. 2006 Sep 29;313(5795):1935-42. doi: 10.1126/science.1131127. Epub 2006 Sep 7.

Abstract

The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA). A metal ion stabilizes a kink in the mRNA that demarcates the boundary between A and P sites, which is potentially important to prevent slippage of mRNA. Metal ions also stabilize the intersubunit interface. The interactions of E-site tRNA with the 50S subunit have both similarities and differences compared to those in the archaeal ribosome. The structure also rationalizes much biochemical and genetic data on translation.

Publication types

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

MeSH terms

  • Anticodon
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Codon
  • Crystallization
  • Crystallography, X-Ray
  • Magnesium / metabolism
  • Models, Molecular
  • Nucleic Acid Conformation
  • Peptidyl Transferases / chemistry
  • Peptidyl Transferases / metabolism
  • Protein Biosynthesis
  • Protein Conformation
  • RNA, Bacterial / chemistry
  • RNA, Bacterial / metabolism
  • RNA, Messenger / chemistry
  • RNA, Messenger / metabolism*
  • RNA, Transfer / chemistry
  • RNA, Transfer / metabolism*
  • RNA, Transfer, Met / chemistry
  • RNA, Transfer, Met / metabolism
  • RNA, Transfer, Phe / chemistry
  • RNA, Transfer, Phe / metabolism
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / metabolism
  • Ribosomes / chemistry*
  • Ribosomes / metabolism
  • Ribosomes / ultrastructure*
  • Thermus thermophilus / chemistry*
  • Thermus thermophilus / ultrastructure

Substances

  • Anticodon
  • Bacterial Proteins
  • Codon
  • RNA, Bacterial
  • RNA, Messenger
  • RNA, Transfer, Met
  • RNA, Transfer, Phe
  • Ribosomal Proteins
  • tRNA, formylmethionine-
  • RNA, Transfer
  • Peptidyl Transferases
  • Magnesium

Associated data

  • PDB/2J00
  • PDB/2J01
  • PDB/2J02
  • PDB/2J03