8CNT

Structure of the DEAH-box helicase Prp16 in complex with ADP

8CNT の概要

• エントリーDOI: 10.2210/pdb8cnt/pdb
• 分子名称: Pre-mRNA splicing factor ATP-dependent RNA helicase prp16-like protein, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: deah-box helicase, hydrolase
• 由来する生物種: Thermochaetoides thermophila DSM 1495
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 72265.00

構造登録者

Garbers, T.B.,Neumann, P.,Ficner, R. (登録日: 2023-02-24, 公開日: 2023-08-23)

主引用文献

Garbers, T.B.,Enders, M.,Neumann, P.,Ficner, R.
Crystal structure of Prp16 in complex with ADP.
Acta Crystallogr.,Sect.F, 79:200-207, 2023

PubMed Abstract: 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 Å resolution. Comparison with the other spliceosomal DEAH-box helicases Prp2, Prp22 and Prp43 reveals an overall identical domain architecture. The β-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.

PubMed: 37548918
DOI: 10.1107/S2053230X23005721

実験手法

X-RAY DIFFRACTION (1.9 Å)