7QGG
Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state
This is a non-PDB format compatible entry.
Summary for 7QGG
| Entry DOI | 10.2210/pdb7qgg/pdb |
| EMDB information | 13954 |
| Descriptor | RNA (1872-MER), 40S ribosomal protein S11, 40S ribosomal protein S15, ... (87 entities in total) |
| Functional Keywords | ribosome, rna granule, rat |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 84 |
| Total formula weight | 3778136.70 |
| Authors | Pulk, A.,Kipper, K.,Mansour, A. (deposition date: 2021-12-08, release date: 2022-10-26, Last modification date: 2024-10-23) |
| Primary citation | Kipper, K.,Mansour, A.,Pulk, A. Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state. J.Mol.Biol., 434:167801-167801, 2022 Cited by PubMed Abstract: The polarized cell morphology of neurons dictates many neuronal processes, including the axodendridic transport of specific mRNAs and subsequent translation. mRNAs together with ribosomes and RNA-binding proteins form RNA granules that are targeted to axodendrites for localized translation in neurons. It has been established that localized protein synthesis in neurons is essential for long-term memory formation, synaptic plasticity, and neurodegeneration. We have used proteomics and electron microscopy to characterize neuronal RNA granules (nRNAg) isolated from rat brain tissues or human neuroblastoma. We show that ribosome-containing RNA granules are morula-like structures when visualized by electron microscopy. Crosslinking-coupled mass-spectrometry identified a potential G3BP2 binding site on the ribosome near the eIF3d-binding site on the 40S ribosomal subunit. We used cryo-EM to resolve the structure of the ribosome-component of nRNAg. The cryo-EM reveals that predominant particles in nRNAg are 80S ribosomes, resembling the pre-translocation state where tRNA's are in the hybrid A/P and P/E site. We also describe a new kind of principal motion of the ribosome, which we call the rocking motion. PubMed: 36038000DOI: 10.1016/j.jmb.2022.167801 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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