6EML

Cryo-EM structure of a late pre-40S ribosomal subunit from Saccharomyces cerevisiae

Summary for 6EML

• Entry DOI: 10.2210/pdb6eml/pdb
• EMDB information: 3886
• Descriptor: pre-18S ribosomal RNA, 40S ribosomal protein S28-B, Ubiquitin-40S ribosomal protein S31, ... (32 entities in total)
• Functional Keywords: ribosome, biogenesis, small subunit, 40s
• Biological source: Saccharomyces cerevisiae S288c; More
• Total number of polymer chains: 32
• Total formula weight: 1292457.95

Authors

Heuer, A.,Thomson, E.,Schmidt, C.,Berninghausen, O.,Becker, T.,Hurt, E.,Beckmann, R. (deposition date: 2017-10-02, release date: 2017-11-29, Last modification date: 2024-05-08)

Primary citation

Heuer, A.,Thomson, E.,Schmidt, C.,Berninghausen, O.,Becker, T.,Hurt, E.,Beckmann, R.
Cryo-EM structure of a late pre-40S ribosomal subunit fromSaccharomyces cerevisiae.
Elife, 6:-, 2017

PubMed Abstract: Mechanistic understanding of eukaryotic ribosome formation requires a detailed structural knowledge of the numerous assembly intermediates, generated along a complex pathway. Here, we present the structure of a late pre-40S particle at 3.6 Å resolution, revealing in molecular detail how assembly factors regulate the timely folding of pre-18S rRNA. The structure shows that, rather than sterically blocking 40S translational active sites, the associated assembly factors Tsr1, Enp1, Rio2 and Pno1 collectively preclude their final maturation, thereby preventing untimely tRNA and mRNA binding and error prone translation. Moreover, the structure explains how Pno1 coordinates the 3'end cleavage of the 18S rRNA by Nob1 and how the late factor's removal in the cytoplasm ensures the structural integrity of the maturing 40S subunit.

PubMed: 29155690
DOI: 10.7554/eLife.30189

Experimental method

ELECTRON MICROSCOPY (3.6 Å)