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5WSG

Cryo-EM structure of the Catalytic Step II spliceosome (C* complex) at 4.0 angstrom resolution

Summary for 5WSG
Entry DOI10.2210/pdb5wsg/pdb
EMDB information6684
DescriptorPre-mRNA-splicing factor 8, Pre-mRNA-splicing factor CWC22, 5'-exon, ... (38 entities in total)
Functional Keywordscatalytic step ii spliceosome, c* spliceosome, rna binding protein-rna complex, rna binding protein/rna
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Total number of polymer chains45
Total formula weight2090498.41
Authors
Yan, C.,Wan, R.,Bai, R.,Huang, G.,Shi, Y. (deposition date: 2016-12-07, release date: 2017-01-25, Last modification date: 2025-07-02)
Primary citationYan, C.,Wan, R.,Bai, R.,Huang, G.,Shi, Y.
Structure of a yeast step II catalytically activated spliceosome
Science, 355:149-155, 2017
Cited by
PubMed Abstract: Each cycle of precursor messenger RNA (pre-mRNA) splicing comprises two sequential reactions, first freeing the 5' exon and generating an intron lariat-3' exon and then ligating the two exons and releasing the intron lariat. The second reaction is executed by the step II catalytically activated spliceosome (known as the C* complex). Here, we present the cryo-electron microscopy structure of a C* complex from Saccharomyces cerevisiae at an average resolution of 4.0 angstroms. Compared with the preceding spliceosomal complex (C complex), the lariat junction has been translocated by 15 to 20 angstroms to vacate space for the incoming 3'-exon sequences. The step I splicing factors Cwc25 and Yju2 have been dissociated from the active site. Two catalytic motifs from Prp8 (the 1585 loop and the β finger of the ribonuclease H-like domain), along with the step II splicing factors Prp17 and Prp18 and other surrounding proteins, are poised to assist the second transesterification. These structural features, together with those reported for other spliceosomal complexes, yield a near-complete mechanistic picture on the splicing cycle.
PubMed: 27980089
DOI: 10.1126/science.aak9979
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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