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TitleMolecular architecture of the Saccharomyces cerevisiae activated spliceosome.
Journal, issue, pagesScience, Vol. 353, Issue 6306, Page 1399-1405, Year 2016
Publish dateSep 23, 2016
AuthorsReinhard Rauhut / Patrizia Fabrizio / Olexandr Dybkov / Klaus Hartmuth / Vladimir Pena / Ashwin Chari / Vinay Kumar / Chung-Tien Lee / Henning Urlaub / Berthold Kastner / Holger Stark / Reinhard Lührmann /
PubMed AbstractThe activated spliceosome (B) is in a catalytically inactive state and is remodeled into a catalytically active machine by the RNA helicase Prp2, but the mechanism is unclear. Here, we describe a 3D ...The activated spliceosome (B) is in a catalytically inactive state and is remodeled into a catalytically active machine by the RNA helicase Prp2, but the mechanism is unclear. Here, we describe a 3D electron cryomicroscopy structure of the Saccharomyces cerevisiae B complex at 5.8-angstrom resolution. Our model reveals that in B, the catalytic U2/U6 RNA-Prp8 ribonucleoprotein core is already established, and the 5' splice site (ss) is oriented for step 1 catalysis but occluded by protein. The first-step nucleophile-the branchsite adenosine-is sequestered within the Hsh155 HEAT domain and is held 50 angstroms away from the 5'ss. Our structure suggests that Prp2 adenosine triphosphatase-mediated remodeling leads to conformational changes in Hsh155's HEAT domain that liberate the first-step reactants for catalysis.
External linksScience / PubMed:27562955
MethodsEM (single particle)
Resolution5.8 Å
Structure data

4099

5lqw

EMDB-4099: Yeast activated spliceosomal B complex
PDB-5lqw: yeast activated spliceosome
Method: EM (single particle) / Resolution: 5.8 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsSPLICING / activated spliceosome / spliceosome / pre-mRNA splicing

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