5IVL

CshA Helicase

5IVL の概要

• エントリーDOI: 10.2210/pdb5ivl/pdb
• 分子名称: DEAD-box ATP-dependent RNA helicase CshA, SULFATE ION (3 entities in total)
• 機能のキーワード: rec-a like domain dead-box helicase, hydrolase
• 由来する生物種: Geobacillus stearothermophilus 10
• 細胞内の位置: Cytoplasm : A0A0K2H973
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97125.92

構造登録者

Huen, J.,Lin, C.-L.,Yi, W.-L.,Li, C.-L.,Yuan, H. (登録日: 2016-03-21, 公開日: 2017-03-22, 最終更新日: 2023-11-08)

主引用文献

Huen, J.,Lin, C.-L.,Golzarroshan, B.,Yi, W.-L.,Yang, W.Z.,Yuan, H.S.
Structural Insights into a Unique Dimeric DEAD-Box Helicase CshA that Promotes RNA Decay.
Structure, 25:469-481, 2017

PubMed Abstract: CshA is a dimeric DEAD-box helicase that cooperates with ribonucleases for mRNA turnover. The molecular mechanism for how a dimeric DEAD-box helicase aids in RNA decay remains unknown. Here, we report the crystal structure and small-angle X-ray scattering solution structure of the CshA from Geobacillus stearothermophilus. In contrast to typical monomeric DEAD-box helicases, CshA is exclusively a dimeric protein with the RecA-like domains of each protomer forming a V-shaped structure. We show that the C-terminal domains protruding outward from the tip of the V-shaped structure is critical for mediating strong RNA binding and is crucial for efficient RNA-dependent ATP hydrolysis. We also show that RNA remains bound with CshA during ATP hydrolysis cycles and thus bulk RNAs could be unwound and degraded in a processive manner through cooperation between exoribonucleases and CshA. A dimeric helicase is hence preserved in RNA-degrading machinery for efficient RNA turnover in prokaryotes and eukaryotes.

PubMed: 28238534
DOI: 10.1016/j.str.2017.01.012

実験手法

X-RAY DIFFRACTION (2.3 Å)