Literature summary for 3.6.4.13 extracted from

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 (2017), Structure, 25, 1795-1808.e5 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of CsdA_218-445 is determined by X-ray diffraction and refined to an R factor of 0.225, with an Rfree of 0.268 at a resolution of 2.3 A by molecular replacement using Hera (PDB ID 3EAQ) as the model. The structure of CsdA_218-445 includes two RecA-like domains (RecA2) and two DDs, which form a V-shape dimer. The V-shape conformation of the CsdA_218-445 dimer in solution is further confirmed by SAXS experiments. Conformational flexibilities of CsdA_1-445 and CsdA_FL are revealed by SAXS	Escherichia coli

Crystallization (Comment)

Organism

structure of CsdA_218-445 is determined by X-ray diffraction and refined to an R factor of 0.225, with an Rfree of 0.268 at a resolution of 2.3 A by molecular replacement using Hera (PDB ID 3EAQ) as the model. The structure of CsdA_218-445 includes two RecA-like domains (RecA2) and two DDs, which form a V-shape dimer. The V-shape conformation of the CsdA_218-445 dimer in solution is further confirmed by SAXS experiments. Conformational flexibilities of CsdA_1-445 and CsdA_FL are revealed by SAXS

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Escherichia coli	-	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9P6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Escherichia coli	ADP + phosphate	-	?
additional information	analysis of ATPase and unwinding activities of CsdA_564 and CsdA_1-445, and of RNA-binding properties of the C-terminal regions of CsdA and CsdA_RNA-binding domain, overview	Escherichia coli	?	-	-

Subunits

Subunits	Comment	Organism
dimer	the helicase core of CsdA is comprised of two RecA-like domains (RecA1 and RecA2) joined by a flexible linker and contains all conserved motifs, two previously auxiliary domains are found: a dimerization domain (DD) and an RNA-binding domain (RBD), conformational flexibilities of the helicase core domains and C-terminal regions, enzyme domain structure, three-dimensional modelling, detailed overview. DD is indispensable for stabilizing the CsdA dimeric structure. Structure comparisons	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ATP-dependent RNA helicase	-	Escherichia coli
cold-shock DEAD-box protein A	-	Escherichia coli
CsdA	-	Escherichia coli
DeaD	-	Escherichia coli
DEAD-box RNA helicase	-	Escherichia coli
RNA helicase CsdA	-	Escherichia coli

General Information

General Information	Comment	Organism
evolution	DEAD-box proteins belong to a ubiquitous family of RNA helicases, which are widely found from prokaryotes to eukaryotes and participate in multiple cellular processes, such as premRNA splicing, translation initiation, modulating RNA-protein complexes, RNA decay, and ribosome biogenesis. Sequence alignment and architecture of different DEAD-Box proteins, overview	Escherichia coli
additional information	the long, flexible C-terminal regions of CsdA are essential for high enzymatic activity and strong RNA-binding affinity, and the RNA-binding domain prefers binding single-stranded G-rich RNA. CsdA functions as a stable dimer at low temperature. The C-terminal regions are critical for RNA binding and efficient enzymatic activities. CsdA_RBD can 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, structure of dimeric RNA helicase CsdA and indispensable role of its C-terminal regions, overview	Escherichia coli