5YLZ

Cryo-EM Structure of the Post-catalytic Spliceosome from Saccharomyces cerevisiae at 3.6 angstrom

Summary for 5YLZ

• Entry DOI: 10.2210/pdb5ylz/pdb
• EMDB information: 6684 6839
• Descriptor: Pre-mRNA-splicing factor 8, Pre-mRNA-splicing factor CEF1, Pre-mRNA-splicing factor SYF2, ... (37 entities in total)
• Functional Keywords: post-catalytic spliceosome (p complex), rna splicing, exon ligation, spliceosome, splicing
• Biological source: Saccharomyces cerevisiae S288c (Baker's yeast); More
• Total number of polymer chains: 43
• Total formula weight: 2285797.78

Authors

Wan, R.,Yan, C.,Bai, R.,Lei, J.,Shi, Y. (deposition date: 2017-10-20, release date: 2018-07-18, Last modification date: 2024-03-27)

Primary citation

Bai, R.,Yan, C.,Wan, R.,Lei, J.,Shi, Y.
Structure of the Post-catalytic Spliceosome from Saccharomyces cerevisiae
Cell, 171:1589-1598.e8, 2017

PubMed Abstract: Removal of an intron from a pre-mRNA by the spliceosome results in the ligation of two exons in the post-catalytic spliceosome (known as the P complex). Here, we present a cryo-EM structure of the P complex from Saccharomyces cerevisiae at an average resolution of 3.6 Å. The ligated exon is held in the active site through RNA-RNA contacts. Three bases at the 3' end of the 5' exon remain anchored to loop I of U5 small nuclear RNA, and the conserved AG nucleotides of the 3'-splice site (3'SS) are specifically recognized by the invariant adenine of the branch point sequence, the guanine base at the 5' end of the 5'SS, and an adenine base of U6 snRNA. The 3'SS is stabilized through an interaction with the 1585-loop of Prp8. The P complex structure provides a view on splice junction formation critical for understanding the complete splicing cycle.

PubMed: 29153833
DOI: 10.1016/j.cell.2017.10.038

Experimental method

ELECTRON MICROSCOPY (3.6 Å)