Structural basis for mRNA and tRNA positioning on the ribosome

Proc Natl Acad Sci U S A. 2006 Oct 24;103(43):15830-4. doi: 10.1073/pnas.0607541103. Epub 2006 Oct 12.

Abstract

Protein synthesis requires the accurate positioning of mRNA and tRNA in the peptidyl-tRNA site of the ribosome. Here we describe x-ray crystal structures of the intact bacterial ribosome from Escherichia coli in a complex with mRNA and the anticodon stem-loop of P-site tRNA. At 3.5-A resolution, these structures reveal rearrangements in the intact ribosome that clamp P-site tRNA and mRNA on the small ribosomal subunit. Binding of the anticodon stem-loop of P-site tRNA to the ribosome is sufficient to lock the head of the small ribosomal subunit in a single conformation, thereby preventing movement of mRNA and tRNA before mRNA decoding.

Publication types

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

MeSH terms

  • Base Sequence
  • Crystallography, X-Ray
  • Escherichia coli / chemistry
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Binding
  • RNA, Messenger / chemistry
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Transfer / chemistry*
  • RNA, Transfer / genetics
  • RNA, Transfer / metabolism*
  • Ribosomal Proteins / chemistry
  • Ribosomal Proteins / metabolism
  • Ribosomes / chemistry
  • Ribosomes / genetics*
  • Ribosomes / metabolism*

Substances

  • RNA, Messenger
  • Ribosomal Proteins
  • RNA, Transfer

Associated data

  • PDB/2I2P
  • PDB/2I2T
  • PDB/2I2U
  • PDB/2I2V