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Solution structure of the E. coli 70S ribosome at 11.5 A resolution.

Over 73,000 projections of the E. coli ribosome bound with formyl-methionyl initiator tRNAf(Met) were used to obtain an 11.5 A cryo-electron microscopy map of the complex. This map allows identification of RNA helices, peripheral proteins, and intersubunit bridges. Comparison of double-stranded RNA regions and positions of proteins identified in both cryo-EM and X-ray maps indicates good overall agreement but points to rearrangements of ribosomal components required for the subunit association. Fitting of known components of the 50S stalk base region into the map defines the architecture of the GTPase-associated center and reveals a major change in the orientation of the alpha-sarcin-ricin loop. Analysis of the bridging connections between the subunits provides insight into the dynamic signaling mechanism between the ribosomal subunits.

Pubmed ID: 10721991

Authors

  • Gabashvili IS
  • Agrawal RK
  • Spahn CM
  • Grassucci RA
  • Svergun DI
  • Frank J
  • Penczek P

Journal

Cell

Publication Data

March 3, 2000

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM55440
  • Agency: NIGMS NIH HHS, Id: R37 GM29169

Mesh Terms

  • Bacterial Proteins
  • Cryoelectron Microscopy
  • Escherichia coli
  • GTP Phosphohydrolases
  • Image Processing, Computer-Assisted
  • Macromolecular Substances
  • Peptide Elongation Factor G
  • RNA, Bacterial
  • RNA, Ribosomal
  • RNA, Transfer, Met
  • Ribosomal Proteins
  • Ribosomes
  • Solutions