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-Structure paper
Title | Three-dimensional structures of translating ribosomes by Cryo-EM. |
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Journal, issue, pages | Mol Cell, Vol. 14, Issue 1, Page 57-66, Year 2004 |
Publish date | Apr 9, 2004 |
Authors | Robert J C Gilbert / Paola Fucini / Sean Connell / Stephen D Fuller / Knud H Nierhaus / Carol V Robinson / Christopher M Dobson / David I Stuart / |
PubMed Abstract | Cryo-electron microscopy and image reconstruction techniques have been used to obtain three-dimensional maps for E. coli ribosomes stalled following translation of three representative proteins. ...Cryo-electron microscopy and image reconstruction techniques have been used to obtain three-dimensional maps for E. coli ribosomes stalled following translation of three representative proteins. Comparisons of these electron density maps, at resolutions of between 13 and 16 A, with that of a nontranslating ribosome pinpoint specific structural differences in stalled ribosomes and identify additional material, including tRNAs and mRNA. In addition, the tunnel through the large subunit, the anticipated exit route of newly synthesized proteins, is partially occluded in all the stalled ribosome structures. This observation suggests that significant segments of the nascent polypeptide chains examined here could be located within an expanded tunnel, perhaps in a rudimentary globular conformation. Such behavior could be an important aspect of the folding of at least some proteins in the cellular environment. |
External links | Mol Cell / PubMed:15068803 |
Methods | EM (single particle) |
Resolution | 13.2 - 16.0 Å |
Structure data | EMDB-1068: EMDB-1070: EMDB-1071: EMDB-1072: EMDB-1073: |
Source |
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