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8RXH

CRYO-EM STRUCTURE OF LEISHMANIA MAJOR 80S RIBOSOME WITH A/P/E-site tRNA AND mRNA : PARENTAL STRAIN

This is a non-PDB format compatible entry.
Summary for 8RXH
Entry DOI10.2210/pdb8rxh/pdb
EMDB information19576
DescriptorLSUa_rRNA_chain_1, Putative ribosomal protein L3, Putative ribosomal protein L1a, ... (95 entities in total)
Functional Keywordscryo-em, leishmania major, 80s, ribosome
Biological sourceLeishmania major strain Friedlin
More
Total number of polymer chains89
Total formula weight3627044.50
Authors
Rajan, K.S.,Yonath, A. (deposition date: 2024-02-07, release date: 2024-05-15, Last modification date: 2024-11-20)
Primary citationRajan, K.S.,Aryal, S.,Hiregange, D.G.,Bashan, A.,Madmoni, H.,Olami, M.,Doniger, T.,Cohen-Chalamish, S.,Pescher, P.,Taoka, M.,Nobe, Y.,Fedorenko, A.,Bose, T.,Zimermann, E.,Prina, E.,Aharon-Hefetz, N.,Pilpel, Y.,Isobe, T.,Unger, R.,Spath, G.F.,Yonath, A.,Michaeli, S.
Structural and mechanistic insights into the function of Leishmania ribosome lacking a single pseudouridine modification.
Cell Rep, 43:114203-114203, 2024
Cited by
PubMed Abstract: Leishmania is the causative agent of cutaneous and visceral diseases affecting millions of individuals worldwide. Pseudouridine (Ψ), the most abundant modification on rRNA, changes during the parasite life cycle. Alterations in the level of a specific Ψ in helix 69 (H69) affected ribosome function. To decipher the molecular mechanism of this phenotype, we determine the structure of ribosomes lacking the single Ψ and its parental strain at ∼2.4-3 Å resolution using cryo-EM. Our findings demonstrate the significance of a single Ψ on H69 to its structure and the importance for its interactions with helix 44 and specific tRNAs. Our study suggests that rRNA modification affects translation of mRNAs carrying codon bias due to selective accommodation of tRNAs by the ribosome. Based on the high-resolution structures, we propose a mechanism explaining how the ribosome selects specific tRNAs.
PubMed: 38722744
DOI: 10.1016/j.celrep.2024.114203
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.93 Å)
Structure validation

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PDB entries from 2024-11-20

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