3JCS

2.8 Angstrom cryo-EM structure of the large ribosomal subunit from the eukaryotic parasite Leishmania

This is a non-PDB format compatible entry.

Summary for 3JCS

• Entry DOI: 10.2210/pdb3jcs/pdb
• EMDB information: 6583
• Descriptor: 26S alpha ribosomal RNA, ribosomal protein L3, ribosomal protein L4, ... (50 entities in total)
• Functional Keywords: leishmania donovani, ribosome, the large ribosomal subunit, eukaryotic parasite
• Biological source: Leishmania donovani; More
• Total number of polymer chains: 48
• Total formula weight: 2170515.34

Authors

Shalev-Benami, M.,Zhang, Y.,Matzov, D.,Halfon, Y.,Zackay, A.,Rozenberg, H.,Zimmerman, E.,Bashan, A.,Jaffe, C.L.,Yonath, A.,Skiniotis, G. (deposition date: 2016-01-21, release date: 2016-07-20, Last modification date: 2018-07-18)

Primary citation

Shalev-Benami, M.,Zhang, Y.,Matzov, D.,Halfon, Y.,Zackay, A.,Rozenberg, H.,Zimmerman, E.,Bashan, A.,Jaffe, C.L.,Yonath, A.,Skiniotis, G.
2.8- angstrom Cryo-EM Structure of the Large Ribosomal Subunit from the Eukaryotic Parasite Leishmania.
Cell Rep, 16:288-294, 2016

PubMed Abstract: Leishmania is a single-cell eukaryotic parasite of the Trypanosomatidae family, whose members cause an array of tropical diseases. The often fatal outcome of infections, lack of effective vaccines, limited selection of therapeutic drugs, and emerging resistant strains, underline the need to develop strategies to combat these pathogens. The Trypanosomatid ribosome has recently been highlighted as a promising therapeutic target due to structural features that are distinct from other eukaryotes. Here, we present the 2.8-Å resolution structure of the Leishmania donovani large ribosomal subunit (LSU) derived from a cryo-EM map, further enabling the structural observation of eukaryotic rRNA modifications that play a significant role in ribosome assembly and function. The structure illustrates the unique fragmented nature of leishmanial LSU rRNA and highlights the irregular distribution of rRNA modifications in Leishmania, a characteristic with implications for anti-parasitic drug development.

PubMed: 27373148
DOI: 10.1016/j.celrep.2016.06.014

Experimental method

ELECTRON MICROSCOPY (2.8 Å)