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Journal Article

Structure and conformational dynamics of the human spliceosomal Bact complex.

MPS-Authors
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Haselbach,  D.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Komarov,  I.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Agafonov,  D. E.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Hartmuth,  K.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Graf,  B.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Dybkov,  O.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Kastner,  B.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Lührmann,  R.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

2529734.pdf
(Publisher version), 7MB

Supplementary Material (public)

2529734_Suppl_1.pdf
(Supplementary material), 522KB

2529734_Suppl_2.xlsx
(Supplementary material), 388KB

2529734_Suppl_3.pdf
(Supplementary material), 21KB

2529734_Suppl_4.mp4
(Supplementary material), 16MB

Citation

Haselbach, D., Komarov, I., Agafonov, D. E., Hartmuth, K., Graf, B., Dybkov, O., et al. (2018). Structure and conformational dynamics of the human spliceosomal Bact complex. Cell, 172(3), 454-464, e1-e5. doi:10.1016/j.cell.2018.01.010.


Cite as: http://hdl.handle.net/21.11116/0000-0000-3A6F-4
Abstract
The spliceosome is a highly dynamic macromolecular complex that precisely excises introns from pre-mRNA. Here we report the cryo-EM 3D structure of the human Bact spliceosome at 3.4 Å resolution. In the Bact state, the spliceosome is activated but not catalytically primed, so that it is functionally blocked prior to the first catalytic step of splicing. The spliceosomal core is similar to the yeast Bact spliceosome; important differences include the presence of the RNA helicase aquarius and peptidyl prolyl isomerases. To examine the overall dynamic behavior of the purified spliceosome, we developed a principal component analysis-based approach. Calculating the energy landscape revealed eight major conformational states, which we refined to higher resolution. Conformational differences of the highly flexible structural components between these eight states reveal how spliceosomal components contribute to the assembly of the spliceosome, allowing it to generate a dynamic interaction network required for its subsequent catalytic activation.