5T2A

CryoEM structure of the Leishmania donovani 80S ribosome at 2.9 Angstrom resolution

This is a non-PDB format compatible entry.

Summary for 5T2A

• Entry DOI: 10.2210/pdb5t2a/pdb
• Related: 5T2C
• EMDB information: 8343 8345
• Descriptor: LSU-alpha, uL16, uL5, ... (80 entities in total)
• Functional Keywords: ribosome, leishmania donovani
• Biological source: Leishmania donovani; More
• Total number of polymer chains: 80
• Total formula weight: 3469652.12

Authors

Zhang, X.,Lai, M.,Zhou, Z.H. (deposition date: 2016-08-23, release date: 2017-01-25, Last modification date: 2024-11-13)

Primary citation

Zhang, X.,Lai, M.,Chang, W.,Yu, I.,Ding, K.,Mrazek, J.,Ng, H.L.,Yang, O.O.,Maslov, D.A.,Zhou, Z.H.
Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes.
Nat Commun, 7:13223-13223, 2016

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-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.

PubMed: 27752045
DOI: 10.1038/ncomms13223

Experimental method

ELECTRON MICROSCOPY (2.9 Å)