7DCR

cryo-EM structure of the DEAH-box helicase Prp2 in complex with its coactivator Spp2

Summary for 7DCR

• Entry DOI: 10.2210/pdb7dcr/pdb
• EMDB information: 30640
• Descriptor: PRP2 isoform 1, Pre-mRNA-splicing factor SPP2 (2 entities in total)
• Functional Keywords: spliceosome, rna splicing, bact complex, deah-box atpase/helicase, prp2, spp2, splicing
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 120632.87

Authors

Bai, R.,Wan, R.,Yan, C.,Jia, Q.,Zhang, P.,Lei, J.,Shi, Y. (deposition date: 2020-10-26, release date: 2021-01-06, Last modification date: 2024-03-27)

Primary citation

Bai, R.,Wan, R.,Yan, C.,Jia, Q.,Lei, J.,Shi, Y.
Mechanism of spliceosome remodeling by the ATPase/helicase Prp2 and its coactivator Spp2.
Science, 371:-, 2021

PubMed Abstract: Spliceosome remodeling, executed by conserved adenosine triphosphatase (ATPase)/helicases including Prp2, enables precursor messenger RNA (pre-mRNA) splicing. However, the structural basis for the function of the ATPase/helicases remains poorly understood. Here, we report atomic structures of Prp2 in isolation, Prp2 complexed with its coactivator Spp2, and Prp2-loaded activated spliceosome and the results of structure-guided biochemical analysis. Prp2 weakly associates with the spliceosome and cannot function without Spp2, which stably associates with Prp2 and anchors on the spliceosome, thus tethering Prp2 to the activated spliceosome and allowing Prp2 to function. Pre-mRNA is loaded into a featured channel between the N and C halves of Prp2, where Leu from the N half and Arg from the C half prevent backward sliding of pre-mRNA toward its 5'-end. Adenosine 5'-triphosphate binding and hydrolysis trigger interdomain movement in Prp2, which drives unidirectional stepwise translocation of pre-mRNA toward its 3'-end. These conserved mechanisms explain the coupling of spliceosome remodeling to pre-mRNA splicing.

PubMed: 33243853
DOI: 10.1126/science.abe8863

Experimental method

ELECTRON MICROSCOPY (3.15 Å)