Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8QIE

CRYO-EM STRUCTURE OF LEISHMANIA MAJOR 80S RIBOSOME : LM32Cs1C1 mutant snoRNA overexpression, class 4

This is a non-PDB format compatible entry.
Summary for 8QIE
Entry DOI10.2210/pdb8qie/pdb
EMDB information18437
DescriptorLSUa_rRNA_chain_1, Putative ribosomal protein L3, Putative ribosomal protein L1a, ... (91 entities in total)
Functional Keywordsleishmania major, snorna, ribosome
Biological sourceLeishmania major strain Friedlin
More
Total number of polymer chains86
Total formula weight3564828.20
Authors
Rajan, K.S.,Yonath, A.,Bashan, A. (deposition date: 2023-09-12, release date: 2025-01-01, Last modification date: 2026-07-22)
Primary citationRajan, K.S.,Aryal, S.,Murugeshan, S.,Zhu, Y.,Bashan, A.,Olami, M.,Madmoni, H.,Nobe, Y.,Doniger, T.,Cohen-Chalamish, S.,Prina, E.,Pescher, P.,Beneke, T.,Taoka, M.,Holley, C.L.,Unger, R.,Spath, G.F.,Yonath, A.,Michaeli, S.
A small nucleolar RNA dictates the structure and function of translating ribosomes in Leishmania.
Nat Commun, 2026
Cited by
PubMed Abstract: The most common rRNA modification is 2'-O-methylation. Here, we determine the landscape of 2'-O-methylation in Leishmania, a parasite that cycles between two different hosts, insect and mammalian. We find two 2'-O-methylated positions that are differentially modified during the parasite's two life stages. The deposition of these modifications is guided by snoRNAs. When we perform cytosine base-editing of the snoRNA responsible for guiding one of the two stage-regulated modifications, Am479, we fail to detect ribosomes lacking this modification, suggesting that it is essential. To better understand the role of the snoRNA and its guided modification, we determine the cryo-EM structures of ribosomes from cells overexpressing the guiding snoRNA and compare them to ribosomes from the parental strain. We do not find structural changes around Am479 or in the small subunit rRNA, but observe a difference in H68 of the large subunit rRNA due to a second base-pairing interaction, suggesting a potential chaperone activity for the snoRNA. Based on these results, translatome and tRNA analysis, we propose a mechanism whereby changes in ribosome structure affect the release of specific tRNAs, which correlate with changes in translation of only a subset of mRNAs.
PubMed: 42443220
DOI: 10.1038/s41467-026-75486-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.43 Å)
Structure validation

257179

PDB entries from 2026-07-29

PDB statisticsPDBj update infoContact PDBjnumon