3KX2

Crystal structure of Prp43p in complex with ADP

3KX2 の概要

• エントリーDOI: 10.2210/pdb3kx2/pdb
• 分子名称: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: rec-a domains, ob fold, winged-helix domain, atp-binding, mrna processing, mrna splicing, nucleotide-binding, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Nucleus: P53131
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 176268.51

構造登録者

Nielsen, K.H.,Andersen, G.R.,He, Y. (登録日: 2009-12-02, 公開日: 2010-01-26, 最終更新日: 2024-03-20)

主引用文献

He, Y.,Andersen, G.R.,Nielsen, K.H.
Structural basis for the function of DEAH helicases
Embo Rep., 11:180-186, 2010

PubMed Abstract: DEAH helicases participate in pre-messenger RNA splicing and ribosome biogenesis. The structure of yeast Prp43p-ADP reveals the homology of DEAH helicases to DNA helicases and the presence of an oligonucleotide-binding motif. A beta-hairpin from the second RecA domain is wedged between two carboxy-terminal domains and blocks access to the occluded RNA binding site formed by the RecA domains and a C-terminal domain. ATP binding and hydrolysis are likely to induce conformational changes in the hairpin that are important for RNA unwinding or ribonucleoprotein remodelling. The structure of Prp43p provides the framework for functional and genetic analysis of all DEAH helicases.

PubMed: 20168331
DOI: 10.1038/embor.2010.11

実験手法

X-RAY DIFFRACTION (2.2 Å)