Literature summary for 3.6.4.13 extracted from

Chen, X.; Wang, C.; Zhang, X.; Tian, T.; Zang, J.
Crystal structures of the N-terminal domain of the Staphylococcus aureus DEAD-box RNA helicase CshA and its complex with AMP (2018), Acta Crystallogr. Sect. F, 74, 704-709 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene cshA, recombinant expression of His-tagged enzyme fragment 1-211, comprising the N-terminal RecA-like domain 1, in Escherichia coli strain Rosetta2 (DE3)	Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant N-terminal RecA-like domain 1 of DEAD-box RNA helicase CshA free and in complex with AMP or AMP-PNP, sitting drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 500 mM NaCl, with AMP or AMP-PNP in a molar ratio of 1:5 for the complexes, is mixed with 0.001 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, 30% v/v PEG 4000, at 16°C, X-ray diffraction structure determination and analysis at 1.5 and 1.8 A resolution, respectively, molecular replacement modelling	Staphylococcus aureus

Crystallization (Comment)

Organism

purified recombinant N-terminal RecA-like domain 1 of DEAD-box RNA helicase CshA free and in complex with AMP or AMP-PNP, sitting drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 500 mM NaCl, with AMP or AMP-PNP in a molar ratio of 1:5 for the complexes, is mixed with 0.001 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, 30% v/v PEG 4000, at 16°C, X-ray diffraction structure determination and analysis at 1.5 and 1.8 A resolution, respectively, molecular replacement modelling

Staphylococcus aureus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	requird	Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
ATP + H2O	Staphylococcus aureus	-	ADP + phosphate	-	?
ATP + H2O	Staphylococcus aureus ATCC 700699	-	ADP + phosphate	-	?
ATP + H2O	Staphylococcus aureus Mu50	-	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	Q99SH6	-	-
Staphylococcus aureus ATCC 700699	Q99SH6	-	-
Staphylococcus aureus Mu50	Q99SH6	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme N-terminal RecA-like domain 1 from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration	Staphylococcus aureus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + H2O	-	Staphylococcus aureus	ADP + phosphate	-	?
ATP + H2O	-	Staphylococcus aureus ATCC 700699	ADP + phosphate	-	?
ATP + H2O	-	Staphylococcus aureus Mu50	ADP + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
CshA	-	Staphylococcus aureus
DEAD-box RNA helicase	-	Staphylococcus aureus

General Information

General Information	Comment	Organism
evolution	CshA is a DEAD-box RNA helicase that belongs to the DExD/H-box family of proteins, which generally have an RNA-dependent ATPase activity	Staphylococcus aureus
additional information	the N-terminal RecA-like domain 1 (amino acids 1-211) of DEAD-box RNA helicase CshA adopts a conserved alpha/beta RecA-like structure with seven parallel strands surrounded by nine alpha-helices. The Q motif and motif I are responsible for the binding of the adenine group and phosphate group of AMP, respectively. Motif I undergoes a conformational change upon AMP binding. Essential roles of Phe22 in the Q motif and Lys52 in motif I for binding ATP, indicating a conserved substrate-binding mechanism in SaCshA compared with other DEAD-box RNA helicases. Structure comparisons, overview	Staphylococcus aureus
physiological function	enzyme CshA is a component of the RNA degradosome and plays important roles in RNA turnover	Staphylococcus aureus