6HEG

Crystal structure of Escherichia coli DEAH/RHA helicase HrpB

6HEG の概要

• エントリーDOI: 10.2210/pdb6heg/pdb
• 分子名称: ATP-dependent RNA helicase HrpB, ADENOSINE-5'-DIPHOSPHATE, TETRAFLUOROALUMINATE ION, ... (4 entities in total)
• 機能のキーワード: deah/rha helicase rna helicase, hydrolase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 90347.69

構造登録者

Xin, B.G.,Chen, W.F.,Rety, S.,Dai, Y.X.,Xi, X.G. (登録日: 2018-08-20, 公開日: 2018-09-12, 最終更新日: 2025-10-01)

主引用文献

Xin, B.G.,Chen, W.F.,Rety, S.,Dai, Y.X.,Xi, X.G.
Crystal structure of Escherichia coli DEAH/RHA helicase HrpB.
Biochem. Biophys. Res. Commun., 504:334-339, 2018

PubMed Abstract: RNA helicases are almost ubiquitous important enzymes that take part in multiple aspects of RNA metabolism. Prokaryotes encode fewer RNA helicases than eukaryotes, suggesting that individual prokaryotic RNA helicases may take on multiple roles. The specific functions and molecular mechanisms of bacterial DEAH/RHA helicases are poorly understood, and no structures are available of these bacterial enzymes. Here, we report the first crystal structure of the DEAH/RHA helicase HrpB of Escherichia coli in a complex with ADP•AlF. It showed an atypical globular structure, consisting of two RecA domains, an HA2 domain and an OB domain, similar to eukaryotic DEAH/RHA helicases. Notably, it showed a unique C-terminal extension that has never been reported before. Activity assays indicated that EcHrpB binds RNA but not DNA, and does not exhibit unwinding activity in vitro. Thus, within cells, the EcHrpB may function in helicase activity-independent RNA metabolic processes.

PubMed: 30190128
DOI: 10.1016/j.bbrc.2018.08.191

実験手法

X-RAY DIFFRACTION (3.019 Å)