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  Molecular architecture of the Saccharomyces cerevisiae activated spliceosome.

Rauhut, R., Fabrizio, P., Dybkov, O., Hartmuth, K., Pena, V., Chari, A., et al. (2016). Molecular architecture of the Saccharomyces cerevisiae activated spliceosome. Science, 353(6306), 1399-1405. doi:10.1126/science.aag1906.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-3346-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-0B9D-F
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 Creators:
Rauhut, R.1, Author              
Fabrizio, P.1, Author              
Dybkov, O.1, Author              
Hartmuth, K.1, Author              
Pena, V.2, Author              
Chari, A.3, Author              
Kumar, V.1, Author              
Lee, C. T.4, Author              
Urlaub, H.4, Author              
Kastner, B.1, Author              
Stark, H.3, Author              
Lührmann, R.1, Author              
Affiliations:
1Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
2Research Group of Macromolecular Crystallography, MPI for Biophysical Chemistry, Max Planck Society, ou_2035293              
3Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              
4Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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 Abstract: The activated spliceosome (Bact) 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 S. cerevisiae Bact complex at 5.8 Å resolution. Our model reveals that in Bact 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 Å away from the 5'ss. Our structure suggests that Prp2 ATPase-mediated remodeling leads to conformational changes in Hsh155's HEAT domain that liberate the first step reactants for catalysis.

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Language(s): eng - English
 Dates: 2016-08-252016-09-23
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.aag1906
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 353 (6306) Sequence Number: - Start / End Page: 1399 - 1405 Identifier: -