PMID:9653034
| Citation |
Malhotra, A, Penczek, P, Agrawal, RK, Gabashvili, IS, Grassucci, RA, Jünemann, R, Burkhardt, N, Nierhaus, KH and Frank, J (1998) Escherichia coli 70 S ribosome at 15 A resolution by cryo-electron microscopy: localization of fMet-tRNAfMet and fitting of L1 protein. J. Mol. Biol. 280:103-16 |
|---|---|
| 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-tRNAfMet as directed by an AUG codon containing mRNA. The superior resolution of this three-dimensional map, 14.9 A, 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. |
| Links |
PubMed Online version:10.1006/jmbi.1998.1859 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Cryoultramicrotomy; Crystallography, X-Ray; Escherichia coli/genetics; Image Processing, Computer-Assisted; Microscopy, Electron; Models, Molecular; Nucleic Acid Conformation; Peptides; Protein Conformation; RNA, Transfer/metabolism; RNA, Transfer, Met/chemistry; RNA, Transfer, Met/metabolism; RNA, Transfer, Met/ultrastructure; Ribosomal Proteins/chemistry; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Ribosomes/ultrastructure; Spectroscopy, Fourier Transform Infrared/methods; Thermus thermophilus/metabolism |
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