Escherichia coli 70 S ribosome at 15 Å resolution by cryo-electron microscopy: Localization of fMet-tRNA(f)(Met) and fitting of L1 protein

Arun Malhotra, Pawel Penczek, Rajendra K. Agrawal, Irene S. Gabashvili, Robert A. Grassucci, Ralf Jünemann, Nils Burkhardt, Knud H. Nierhaus, Joachim Frank

Research output: Contribution to journalArticle

160 Scopus citations

Abstract

Cryo-electron microscopy of the ribosome in different binding states with mRNA and tRNA helps unravel the different steps of protein synthesis. Using over 29,000 projections of a ribosome complex in single-particle form, a three-dimensional map of the Escherichia coli 70 S ribosome was obtained in which a single site, the P site, is occupied by fMet-tRNA(f)(MET) as directed by an AUG codon containing mRNA. The superior resolution of this three-dimensional map, 14.9 Å, has made it possible to fit the tRNA X-ray crystal structure directly and unambiguously into the electron density, thus determining the locations of anticodon-codon interaction and peptidyltransferase center of the ribosome. Furthermore, at this resolution, one of the distinctly visible domains corresponding to a ribosomal protein, L1, closely matches with its X-ray structure.

Original languageEnglish (US)
Pages (from-to)103-116
Number of pages14
JournalJournal of molecular biology
Volume280
Issue number1
DOIs
StatePublished - Jul 3 1998
Externally publishedYes

Keywords

  • Cryo-electron microscopy
  • L1 protein
  • Polypeptide exit tunnel
  • Ribosome structure
  • tRNA P-site

ASJC Scopus subject areas

  • Virology

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    Malhotra, A., Penczek, P., Agrawal, R. K., Gabashvili, I. S., Grassucci, R. A., Jünemann, R., Burkhardt, N., Nierhaus, K. H., & Frank, J. (1998). Escherichia coli 70 S ribosome at 15 Å resolution by cryo-electron microscopy: Localization of fMet-tRNA(f)(Met) and fitting of L1 protein. Journal of molecular biology, 280(1), 103-116. https://doi.org/10.1006/jmbi.1998.1859