Xing Zhang / Mason Lai / Winston Chang / Iris Yu / Ke Ding / Jan Mrazek / Hwee L Ng / Otto O Yang / Dmitri A Maslov / Z Hong Zhou /
PubMed Abstract
The recent success in ribosome structure determination by cryoEM has opened the door to defining structural differences between ribosomes of pathogenic organisms and humans and to understand ribosome- ...The recent success in ribosome structure determination by cryoEM has opened the door to defining structural differences between ribosomes of pathogenic organisms and humans and to understand ribosome-targeting antibiotics. Here, by direct electron-counting cryoEM, we have determined the structures of the Leishmania donovani and human ribosomes at 2.9 Å and 3.6 Å, respectively. Our structure of the leishmanial ribosome elucidates the organization of the six fragments of its large subunit rRNA (as opposed to a single 28S rRNA in most eukaryotes, including humans) and reveals atomic details of a unique 20 amino acid extension of the uL13 protein that pins down the ends of three of the rRNA fragments. The structure also fashions many large rRNA expansion segments. Direct comparison of our human and leishmanial ribosome structures at the decoding A-site sheds light on how the bacterial ribosome-targeting drug paromomycin selectively inhibits the eukaryotic L. donovani, but not human, ribosome.
EMDB-8343:Cryo-EM structure of the Leishmania donovani 80S ribosome at 2.9 Angstrom resolution PDB-5t2a:CryoEM structure of the Leishmania donovani 80S ribosome at 2.9 Angstrom resolution Method: EM (single particle) / Resolution: 2.9 Å
EMDB-8345: Cryo-EM structure of the human 80S ribosome at 3.6 Angstrom resolution PDB-5t2c: CryoEM structure of the human ribosome at 3.6 Angstrom resolution Method: EM (single particle) / Resolution: 3.6 Å
Source
leishmania donovani (eukaryote)
homo sapiens (human)
Keywords
RIBOSOME / Leishmania donovani
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Keywords
leishmania donovani (eukaryote)
homo sapiens (human)