5B88

RRM-like domain of DEAD-box protein, CsdA

5B88 の概要

• エントリーDOI: 10.2210/pdb5b88/pdb
• 分子名称: ATP-dependent RNA helicase DeaD (1 entity in total)
• 機能のキーワード: rna binding protein
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9448.83

構造登録者

Xu, L.,Peng, J.,Zhang, J.,Wu, J.,Tang, Y.,Shi, Y. (登録日: 2016-06-13, 公開日: 2017-05-31, 最終更新日: 2024-05-15)

主引用文献

Xu, L.,Wang, L.,Peng, J.,Li, F.,Wu, L.,Zhang, B.,Lv, M.,Zhang, J.,Gong, Q.,Zhang, R.,Zuo, X.,Zhang, Z.,Wu, J.,Tang, Y.,Shi, Y.
Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions.
Structure, 25:1795-1808.e5, 2017

PubMed Abstract: CsdA has been proposed to be essential for the biogenesis of ribosome and gene regulation after cold shock. However, the structure of CsdA and the function of its long C-terminal regions are still unclear. Here, we solved all of the domain structures of CsdA and found two previously uncharacterized auxiliary domains: a dimerization domain (DD) and an RNA-binding domain (RBD). Small-angle X-ray scattering experiments helped to track the conformational flexibilities of the helicase core domains and C-terminal regions. Biochemical assays revealed that DD is indispensable for stabilizing the CsdA dimeric structure. We also demonstrate for the first time that CsdA functions as a stable dimer at low temperature. The C-terminal regions are critical for RNA binding and efficient enzymatic activities. CsdA_RBD could specifically bind to the regions with a preference for single-stranded G-rich RNA, which may help to bring the helicase core to unwind the adjacent duplex.

PubMed: 29107486
DOI: 10.1016/j.str.2017.09.013

実験手法

SOLUTION NMR