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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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 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.5, 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              
3Research Group of Structural Biochemistry and Mechanisms, MPI for Biophysical Chemistry, Max Planck Society, ou_3265855              
4Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              
5Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              

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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: Issued
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 Rev. Type: 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: -