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9HC4

Cryo-EM structure of P. urativorans 70S ribosome with 2 copies of bS20.

This is a non-PDB format compatible entry.
Summary for 9HC4
Entry DOI10.2210/pdb9hc4/pdb
EMDB information52036
DescriptorSmall ribosomal subunit protein uS9, Large ribosomal subunit protein bL17, Large ribosomal subunit protein bL25, ... (52 entities in total)
Functional Keywordsribosome, ribosome heterogeneity, functionally specialized ribosomes, polysome
Biological sourcePsychrobacter urativorans
More
Total number of polymer chains53
Total formula weight2180733.71
Authors
Helena-Bueno, K.,Hill, C.H.,Melnikov, S.V. (deposition date: 2024-11-08, release date: 2025-03-26, Last modification date: 2025-04-02)
Primary citationHelena-Bueno, K.,Kopetschke, S.,Filbeck, S.,Chan, L.I.,Birsan, S.,Basle, A.,Hudson, M.,Pfeffer, S.,Hill, C.H.,Melnikov, S.V.
Structurally heterogeneous ribosomes cooperate in protein synthesis in bacterial cells.
Nat Commun, 16:2751-2751, 2025
Cited by
PubMed Abstract: Ribosome heterogeneity is a paradigm in biology, pertaining to the existence of structurally distinct populations of ribosomes within a single organism or cell. This concept suggests that structurally distinct pools of ribosomes have different functional properties and may be used to translate specific mRNAs. However, it is unknown to what extent structural heterogeneity reflects genuine functional specialization rather than stochastic variations in ribosome assembly. Here, we address this question by combining cryo-electron microscopy and tomography to observe individual structurally heterogeneous ribosomes in bacterial cells. We show that 70% of ribosomes in Psychrobacter urativorans contain a second copy of the ribosomal protein bS20 at a previously unknown binding site on the large ribosomal subunit. We then determine that this second bS20 copy appears to be functionally neutral. This demonstrates that ribosome heterogeneity does not necessarily lead to functional specialization, even when it involves significant variations such as the presence or absence of a ribosomal protein. Instead, we show that heterogeneous ribosomes can cooperate in general protein synthesis rather than specialize in translating discrete populations of mRNA.
PubMed: 40113756
DOI: 10.1038/s41467-025-57955-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

236620

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