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3JB9

Cryo-EM structure of the yeast spliceosome at 3.6 angstrom resolution

Summary for 3JB9
Entry DOI10.2210/pdb3jb9/pdb
EMDB information6413
DescriptorPre-mRNA-splicing factor spp42, Small nuclear ribonucleoprotein G, Pre-mRNA-splicing factor prp5, ... (37 entities in total)
Functional Keywordsspliceosome, u2/u5/u6, lariat, rna binding protein-rna complex, rna binding protein/rna
Biological sourceSchizosaccharomyces pombe 972h- (Fission yeast)
More
Total number of polymer chains43
Total formula weight1789825.08
Authors
Yan, C.,Hang, J.,Wan, R.,Huang, M.,Wong, C.,Shi, Y. (deposition date: 2015-08-09, release date: 2015-09-23, Last modification date: 2024-03-20)
Primary citationYan, C.,Hang, J.,Wan, R.,Huang, M.,Wong, C.,Shi, Y.
Structure of a yeast spliceosome at 3.6-angstrom resolution
Science, 349:1182-1191, 2015
Cited by
PubMed Abstract: Splicing of precursor messenger RNA (pre-mRNA) in yeast is executed by the spliceosome, which consists of five small nuclear ribonucleoproteins (snRNPs), NTC (nineteen complex), NTC-related proteins (NTR), and a number of associated enzymes and cofactors. Here, we report the three-dimensional structure of a Schizosaccharomyces pombe spliceosome at 3.6-angstrom resolution, revealed by means of single-particle cryogenic electron microscopy. This spliceosome contains U2 and U5 snRNPs, NTC, NTR, U6 small nuclear RNA, and an RNA intron lariat. The atomic model includes 10,574 amino acids from 37 proteins and four RNA molecules, with a combined molecular mass of approximately 1.3 megadaltons. Spp42 (Prp8 in Saccharomyces cerevisiae), the key protein component of the U5 snRNP, forms a central scaffold and anchors the catalytic center. Both the morphology and the placement of protein components appear to have evolved to facilitate the dynamic process of pre-mRNA splicing. Our near-atomic-resolution structure of a central spliceosome provides a molecular framework for mechanistic understanding of pre-mRNA splicing.
PubMed: 26292707
DOI: 10.1126/science.aac7629
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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数据于2025-06-25公开中

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