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5XJC

Cryo-EM structure of the human spliceosome just prior to exon ligation at 3.6 angstrom

This is a non-PDB format compatible entry.
Summary for 5XJC
Entry DOI10.2210/pdb5xjc/pdb
EMDB information6721
DescriptorPre-mRNA-processing-splicing factor 8, Crooked neck-like protein 1, Pre-mRNA-splicing factor SPF27, ... (46 entities in total)
Functional Keywordsrna splicing, human spliceosome, c* complex, atomic structure, step 2 factors, ejc, splicing
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains50
Total formula weight2962080.49
Authors
Zhang, X.,Yan, C.,Hang, J.,Finci, I.L.,Lei, J.,Shi, Y. (deposition date: 2017-04-30, release date: 2017-07-05, Last modification date: 2024-11-20)
Primary citationZhang, X.,Yan, C.,Hang, J.,Finci, L.I.,Lei, J.,Shi, Y.
An Atomic Structure of the Human Spliceosome
Cell, 169:918-929.e14, 2017
Cited by
PubMed Abstract: Mechanistic understanding of pre-mRNA splicing requires detailed structural information on various states of the spliceosome. Here we report the cryo electron microscopy (cryo-EM) structure of the human spliceosome just before exon ligation (the C complex) at an average resolution of 3.76 Å. The splicing factor Prp17 stabilizes the active site conformation. The step II factor Slu7 adopts an extended conformation, binds Prp8 and Cwc22, and is poised for selection of the 3'-splice site. Remarkably, the intron lariat traverses through a positively charged central channel of RBM22; this unusual organization suggests mechanisms of intron recruitment, confinement, and release. The protein PRKRIP1 forms a 100-Å α helix linking the distant U2 snRNP to the catalytic center. A 35-residue fragment of the ATPase/helicase Prp22 latches onto Prp8, and the quaternary exon junction complex (EJC) recognizes upstream 5'-exon sequences and associates with Cwc22 and the GTPase Snu114. These structural features reveal important mechanistic insights into exon ligation.
PubMed: 28502770
DOI: 10.1016/j.cell.2017.04.033
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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