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7btb

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Cryo-EM structure of pre-60S ribosome from Saccharomyces cerevisiae rpl4delta63-87 strain at 3.22 Angstroms resolution(state R2)

Structural highlights

7btb is a 10 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.22Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL13A_YEAST

Publication Abstract from PubMed

The nascent polypeptide exit tunnel (NPET) is a major functional center of 60S ribosomal subunits. However, little is known about how the NPET is constructed during ribosome assembly. We utilized molecular genetics, biochemistry, and cryo-electron microscopy (cryo-EM) to investigate the functions of two NPET-associated proteins, ribosomal protein uL4 and assembly factor Nog1, in NPET assembly. Structures of mutant pre-ribosomes lacking the tunnel domain of uL4 reveal a misassembled NPET, including an aberrantly flexible ribosomal RNA helix 74, resulting in at least three different blocks in 60S assembly. Structures of pre-ribosomes lacking the C-terminal extension of Nog1 demonstrate that this extension scaffolds the tunnel domain of uL4 in the NPET to help maintain stability in the core of pre-60S subunits. Our data reveal that uL4 and Nog1 work together in the maturation of ribosomal RNA helix 74, which is required to ensure proper construction of the NPET and 60S ribosomal subunits.

Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel.,Wilson DM, Li Y, LaPeruta A, Gamalinda M, Gao N, Woolford JL Jr Nat Commun. 2020 Oct 9;11(1):5111. doi: 10.1038/s41467-020-18878-8. PMID:33037216^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wilson DM, Li Y, LaPeruta A, Gamalinda M, Gao N, Woolford JL Jr. Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel. Nat Commun. 2020 Oct 9;11(1):5111. PMID:33037216 doi:10.1038/s41467-020-18878-8