7abi

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Human pre-Bact-2 spliceosome

Structural highlights

7abi is a 12 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 8Å
Ligands:GTP, IHP, MG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SNR40_HUMAN Component of the U5 small nuclear ribonucleoprotein (snRNP) complex. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs.[1]

Publication Abstract from PubMed

Spliceosome activation involves extensive protein and RNA rearrangements that lead to formation of a catalytically active U2/U6 RNA structure. At present, little is known about the assembly pathway of the latter and the mechanism whereby proteins aid its proper folding. Here, we report the cryo-electron microscopy structures of two human, activated spliceosome precursors (that is, pre-B(act) complexes) at core resolutions of 3.9 and 4.2 angstroms. These structures elucidate the order of the numerous protein exchanges that occur during activation, the mutually exclusive interactions that ensure the correct order of ribonucleoprotein rearrangements needed to form the U2/U6 catalytic RNA, and the stepwise folding pathway of the latter. Structural comparisons with mature B(act) complexes reveal the molecular mechanism whereby a conformational change in the scaffold protein PRP8 facilitates final three-dimensional folding of the U2/U6 catalytic RNA.

Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation.,Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Luhrmann R Science. 2020 Dec 18;370(6523):eabc3753. doi: 10.1126/science.abc3753. Epub 2020 , Nov 26. PMID:33243851[2]

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

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Citations
10 reviews cite this structure
Regulation of pre-mRNA splicing: roles in physiology and disease, and therapeutic prospects.
Rogalska et al. (2023)
9 more
33 other articles
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See Also

References

  1. ↑ Achsel T, Ahrens K, Brahms H, Teigelkamp S, Luhrmann R. The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein. Mol Cell Biol. 1998 Nov;18(11):6756-66. PMID:9774689
  2. ↑ Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Lührmann R. Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. Science. 2020 Dec 18;370(6523):eabc3753. PMID:33243851 doi:10.1126/science.abc3753

Contents


PDB ID 7abi

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OCA

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