6FF4

human Bact spliceosome core structure

Summary for 6FF4

• Entry DOI: 10.2210/pdb6ff4/pdb
• EMDB information: 4233 4234 4235 4236 4237 4238 4239 4240 4255
• Descriptor: RNA-binding motif protein, X-linked 2, SNW domain-containing protein 1, Pleiotropic regulator 1, ... (32 entities in total)
• Functional Keywords: spliceosome, human, hela, bact, dynamics, splicing
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 28
• Total formula weight: 2229574.34

Authors

Haselbach, D.,Komarov, I.,Agafonov, D.,Hartmuth, K.,Graf, B.,Kastner, B.,Luehrmann, R.,Stark, H. (deposition date: 2018-01-03, release date: 2018-08-29, Last modification date: 2024-11-06)

Primary citation

Haselbach, D.,Komarov, I.,Agafonov, D.E.,Hartmuth, K.,Graf, B.,Dybkov, O.,Urlaub, H.,Kastner, B.,Luhrmann, R.,Stark, H.
Structure and Conformational Dynamics of the Human Spliceosomal BactComplex.
Cell, 172:454-464.e11, 2018

PubMed 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 B spliceosome at 3.4 Å resolution. In the B 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 B 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.

PubMed: 29361316
DOI: 10.1016/j.cell.2018.01.010

Experimental method

ELECTRON MICROSCOPY (3.4 Å)