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9SDQ

Cryo-EM structure of the Arabidopsis thaliana 40S ribosomal subunit (Head)

This is a non-PDB format compatible entry.
Summary for 9SDQ
Entry DOI10.2210/pdb9sdq/pdb
EMDB information54790
DescriptorRNA (500-MER), Small ribosomal subunit protein uS14z/uS14y/uS14x, Small ribosomal subunit protein eS25y, ... (16 entities in total)
Functional Keywordsribosomal 40s subunit -head region, ribosome
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains13
Total formula weight353713.55
Authors
Primary citationKarki, S.,Lu, X.,Paatero, A.O.,Ruonala, R.,Tranter, D.,Guryanov, S.,Rehan, S.,Hellmann, E.,Haakonsson, A.,Butcher, S.J.,Huiskonen, J.T.,Kajander, T.,Helariutta, Y.,Paavilainen, V.O.
Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.
Structure, 2026
Cited by
PubMed Abstract: Translational control of mRNA expression underpins much of post-transcriptional gene expression driving developmental processes in eukaryotes. How ribosomal mRNA translation is executed in plants may be especially important for adapting to an ever-changing environment. Arabidopsis thaliana is the main genetic model organism in plant science, yet structural insights into developmental processes where ribosomal gene expression plays important roles currently remain lacking. Here, we present cryoelectron microscopy (cryo-EM) structures of the Arabidopsis cytosolic ribosome in both translating and non-translating states, which together provide new structural details into how translation of cytosolic mRNAs is coordinated. Our structures reveal detailed information on the interactions of tRNAs, mRNA, and the nascent polypeptide with subunits of the actively translating 80S ribosome and the role of ribosomal RNA methylation in stabilizing ribosomal subunits. The structures provide a foundation for interpreting the functional effects of many mutations of ribosomal proteins affecting phenotypic effects for plant tissue development.
PubMed: 42361795
DOI: 10.1016/j.str.2026.06.001
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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PDB entries from 2026-07-29

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