5H4P

Structural snapshot of cytoplasmic pre-60S ribosomal particles bound with Nmd3, Lsg1, Tif6 and Reh1

This is a non-PDB format compatible entry.

Summary for 5H4P

• Entry DOI: 10.2210/pdb5h4p/pdb
• EMDB information: 9569
• Descriptor: 25S ribosomal RNA, 60S ribosomal protein L8-A, 60S ribosomal protein L9-A, ... (44 entities in total)
• Functional Keywords: pre-60s, nmd3, lsg1, assembly, ribosome
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm : P17076 P05738 P0C0W9 Q12690 P36105 P05748 P26784 P05740 P0CX49 P0CX82 P0CX23 Q02753 P05749 P0CX41 P04449 P04456 P05743 P0C2H6 P02406 P05747 P14120 P0C2H8 P38061 P05744 P87262 P0CX84 P05745 P49166 P49167 P04650 P0CX45 P0CX27 P0CX25 P38861 Q12522 Q06709 P14126 P10664 P26321 Q02326 P05737
• Total number of polymer chains: 44
• Total formula weight: 1945395.35

Authors

Ma, C.,Wu, S.,Li, N.,Chen, Y.,Yan, K.,Li, Z.,Zheng, L.,Lei, J.,Woolford, J.L.,Gao, N. (deposition date: 2016-11-01, release date: 2017-01-25, Last modification date: 2024-03-20)

Primary citation

Ma, C.,Wu, S.,Li, N.,Chen, Y.,Yan, K.,Li, Z.,Zheng, L.,Lei, J.,Woolford, J.L.,Gao, N.
Structural snapshot of cytoplasmic pre-60S ribosomal particles bound by Nmd3, Lsg1, Tif6 and Reh1
Nat. Struct. Mol. Biol., 24:214-220, 2017

PubMed Abstract: A key step in ribosome biogenesis is the nuclear export of pre-ribosomal particles. Nmd3, a highly conserved protein in eukaryotes, is a specific adaptor required for the export of pre-60S particles. Here we used cryo-electron microscopy (cryo-EM) to characterize Saccharomyces cerevisiae pre-60S particles purified with epitope-tagged Nmd3. Our structural analysis indicates that these particles belong to a specific late stage of cytoplasmic pre-60S maturation in which ribosomal proteins uL16, uL10, uL11, eL40 and eL41 are deficient, but ribosome assembly factors Nmd3, Lsg1, Tif6 and Reh1 are present. Nmd3 and Lsg1 are located near the peptidyl-transferase center (PTC). In particular, Nmd3 recognizes the PTC in its near-mature conformation. In contrast, Reh1 is anchored to the exit of the polypeptide tunnel, with its C terminus inserted into the tunnel. These findings pinpoint a structural checkpoint role for Nmd3 in PTC assembly, and provide information about functional and mechanistic roles of these assembly factors in the maturation of the 60S ribosomal subunit.

PubMed: 28112732
DOI: 10.1038/nsmb.3364

Experimental method

ELECTRON MICROSCOPY (3.07 Å)