5GI4

DEAD-box RNA helicase

Summary for 5GI4

• Entry DOI: 10.2210/pdb5gi4/pdb
• Descriptor: ATP-dependent RNA helicase DeaD (2 entities in total)
• Functional Keywords: dimer, reca-like, wild type, rna helicase, hydrolase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 2
• Total formula weight: 51498.67

Authors

Xu, L.,Wang, L.,Li, F.,Wu, L.,Shi, Y. (deposition date: 2016-06-22, release date: 2017-05-31, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.244 Å)