8cnt

Publication Abstract from PubMed

DEAH-box helicases play a crucial role in pre-mRNA splicing as they are responsible for major rearrangements of the spliceosome and are involved in various quality-ensuring steps. Prp16 is the driving force during spliceosomal catalysis, remodeling the C state into the C* state. Here, the first crystal structure of Prp16 from Chaetomium thermophilum in complex with ADP is reported at 1.9 A resolution. Comparison with the other spliceosomal DEAH-box helicases Prp2, Prp22 and Prp43 reveals an overall identical domain architecture. The beta-hairpin, which is a structural element of the RecA2 domain, exhibits a unique position, punctuating its flexibility. Analysis of cryo-EM models of spliceosomal complexes containing Prp16 reveals that these models show Prp16 in its nucleotide-free state, rendering the model presented here the first structure of Prp16 in complex with a nucleotide.

Crystal structure of Prp16 in complex with ADP.,Garbers TB, Enders M, Neumann P, Ficner R Acta Crystallogr F Struct Biol Commun. 2023 Aug 1;79(Pt 8):200-207. doi: , 10.1107/S2053230X23005721. Epub 2023 Jul 25. PMID:37548918^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.