Literature summary for 3.1.26.12 extracted from

Callaghan, A.J.; Grossmann, J.G.; Redko, Y.U.; Ilag, L.L.; Moncrieffe, M.C.; Symmons, M.F.; Robinson, C.V.; McDowall, K.J.; Luisi, B.F.
Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain (2003), Biochemistry, 42, 13848-13855.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of the His-tagged N-terminal RNaseE catalytic N domain, comprising residues 1-529, in strain BL21(DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His-tagged N-terminal RNaseE catalytic N domain, vapour diffusion method, 7 mg/ml protein in solution is mixed in a 1:1 ratio with precipitation solution containing 0.18 M Li2SO4, 0.09 M Tris-HCl, pH 8.5, 27% w/v PEG 4000, and 10% v/v glycerol, X-ray diffraction structure determination and analysis at 3.4 A resolution	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
300000	-	N-terminal catalytic domain homotetramer, analytical ultracentrifugation	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged N-terminal RNaseE catalytic N domain from strain BL21(DE3) by metal affinity chromatography and gel filtration to homogeneity	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5'ACAGUAUUUG-fluorescein + H2O	5' monophosphorylated, 3' fluorescein-labeled synthetic substrate with protective 2'-O-methyl groups at all positions based on the 5' cleavage site of pBR322 RNA I	Escherichia coli	5'ACAGU + AUUUG-fluorescein	-	?
additional information	RNase E acts via a scanning mechanism in processing and degradation of RNA	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
More	the enzymes' conserved N-terminal catalytic domain forms homotetramers binding up to four molecules of specific RNA substrate, the tetramers forms a D2 dihedral symmetry, X-ray scattering, analytical ultracentrifugation, mass spectrometry, and circular dichroism used for structure analysis, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ribonuclease E	-	Escherichia coli
RNase E	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.3	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)