3J0P

Core of mammalian 80S pre-ribosome in complex with tRNAs fitted to a 10.6A cryo-em map: rotated PRE state 1

Summary for 3J0P

• Entry DOI: 10.2210/pdb3j0p/pdb
• Related: 3J0L 3J0O 3J0Q
• EMDB information: 5328
• Descriptor: 40S ribosomal RNA fragment, Ribosomal protein S30, 60S ribosomal RNA fragment, ... (18 entities in total)
• Functional Keywords: mammalia, translation, elongation cycle, trna, ribosome
• Biological source: Oryctolagus cuniculus (rabbit); More
• Total number of polymer chains: 18
• Total formula weight: 247719.64

Authors

Budkevich, T.,Giesebrecht, J.,Altman, R.,Munro, J.,Mielke, T.,Nierhaus, K.,Blanchard, S.,Spahn, C.M. (deposition date: 2011-10-06, release date: 2011-11-16, Last modification date: 2024-02-21)

Primary citation

Budkevich, T.,Giesebrecht, J.,Altman, R.B.,Munro, J.B.,Mielke, T.,Nierhaus, K.H.,Blanchard, S.C.,Spahn, C.M.
Structure and dynamics of the Mammalian ribosomal pretranslocation complex.
Mol.Cell, 44:214-224, 2011

PubMed Abstract: Although the structural core of the ribosome is conserved in all kingdoms of life, eukaryotic ribosomes are significantly larger and more complex than their bacterial counterparts. The extent to which these differences influence the molecular mechanism of translation remains elusive. Multiparticle cryo-electron microscopy and single-molecule FRET investigations of the mammalian pretranslocation complex reveal spontaneous, large-scale conformational changes, including an intersubunit rotation of the ribosomal subunits. Through structurally related processes, tRNA substrates oscillate between classical and at least two distinct hybrid configurations facilitated by localized changes in their L-shaped fold. Hybrid states are favored within the mammalian complex. However, classical tRNA positions can be restored by tRNA binding to the E site or by the eukaryotic-specific antibiotic and translocation inhibitor cycloheximide. These findings reveal critical distinctions in the structural and energetic features of bacterial and mammalian ribosomes, providing a mechanistic basis for divergent translation regulation strategies and species-specific antibiotic action.

PubMed: 22017870
DOI: 10.1016/j.molcel.2011.07.040

Experimental method

ELECTRON MICROSCOPY (10.6 Å)