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8B2L

Cryo-EM structure of the plant 80S ribosome

This is a non-PDB format compatible entry.
Summary for 8B2L
Entry DOI10.2210/pdb8b2l/pdb
EMDB information15806
Descriptor40S ribosomal protein S4, 40S ribosomal protein S24, 40S ribosomal protein S25, ... (88 entities in total)
Functional Keywordsplant, 80s, rrna modifications, ribosome
Biological sourceNicotiana tabacum (common tobacco)
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Total number of polymer chains83
Total formula weight3262704.91
Authors
Smirnova, J.,Loerke, J.,Kleinau, G.,Schmidt, A.,Buerger, J.,Meyer, E.H.,Mielke, T.,Scheerer, P.,Bock, R.,Spahn, C.M.T.,Zoschke, R. (deposition date: 2022-09-14, release date: 2023-08-23, Last modification date: 2024-04-24)
Primary citationSmirnova, J.,Loerke, J.,Kleinau, G.,Schmidt, A.,Burger, J.,Meyer, E.H.,Mielke, T.,Scheerer, P.,Bock, R.,Spahn, C.M.T.,Zoschke, R.
Structure of the actively translating plant 80S ribosome at 2.2 angstrom resolution.
Nat.Plants, 9:987-1000, 2023
Cited by
PubMed Abstract: In plant cells, translation occurs in three compartments: the cytosol, the plastids and the mitochondria. While the structures of the (prokaryotic-type) ribosomes in plastids and mitochondria are well characterized, high-resolution structures of the eukaryotic 80S ribosomes in the cytosol have been lacking. Here the structure of translating tobacco (Nicotiana tabacum) 80S ribosomes was solved by cryo-electron microscopy with a global resolution of 2.2 Å. The ribosome structure includes two tRNAs, decoded mRNA and the nascent peptide chain, thus providing insights into the molecular underpinnings of the cytosolic translation process in plants. The map displays conserved and plant-specific rRNA modifications and the positions of numerous ionic cofactors, and it uncovers the role of monovalent ions in the decoding centre. The model of the plant 80S ribosome enables broad phylogenetic comparisons that reveal commonalities and differences in the ribosomes of plants and those of other eukaryotes, thus putting our knowledge about eukaryotic translation on a firmer footing.
PubMed: 37156858
DOI: 10.1038/s41477-023-01407-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.2 Å)
Structure validation

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