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Updated: Jul 19, 2025

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Published on: December 30, 2016
Crystal structure of Prp16 in complex with ADP
Tim Benedict Garbers1, Marieke Enders1, Piotr Neumann1
1Department of Molecular Structural Biology, Institute of Microbiology and Genetics, GZMB, Georg-August-University Göttingen, Göttingen, Germany.
This study presents the first crystal structure of the DEAH-box helicase Prp16 bound to ADP. This provides new insights into spliceosome remodeling and RNA splicing quality control mechanisms.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- DEAH-box helicases are essential for pre-mRNA splicing, mediating spliceosome rearrangements and quality control.
- Prp16 is a key enzyme that drives spliceosomal catalysis, remodeling the spliceosome from the C to the C* state.
Purpose of the Study:
- To determine the first crystal structure of Prp16 from Chaetomium thermophilum in complex with ADP.
- To compare the structural features of Prp16 with other spliceosomal DEAH-box helicases.
Main Methods:
- X-ray crystallography at 1.9 Å resolution.
- Structural comparison with related proteins.
Main Results:
- The crystal structure of Prp16 in complex with ADP was determined.
- Prp16 shares an identical domain architecture with other spliceosomal DEAH-box helicases (Prp2, Prp22, Prp43).
- A unique β-hairpin in the RecA2 domain highlights Prp16's flexibility.
Conclusions:
- This structure represents the first view of Prp16 bound to a nucleotide, contrasting with previously studied nucleotide-free cryo-EM models.
- The findings offer a structural basis for understanding Prp16's role in spliceosome dynamics and catalysis.
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