Literature summary for 3.1.26.12 extracted from

Schubert, M.; Edge, R.E.; Lario, P.; Cook, M.A.; Strynadka, N.C.; Mackie, G.A.; McIntosh, L.P.
Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces (2004), J. Mol. Biol., 341, 37-54.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of N-terminally His6-tagged wild-type and mutant full-length enzymes, and of isolated N-terminally His6-tagged S1 domain comprising residues 35-125	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant detagged isolated S1 domain, residues 35-125, large crystals grow within 4 weeks in 1.65 mM protein containing solution of 20 mM phosphate, pH 6.5, 50 mM NaCl, and 0.05% w/v NaN3 at 4°C, isomorphous crystals are grown by hanging drop vapour diffusion method at 18°C, 1.3 mM protein in 20 mM HEPES, p 6.5, 50 mM NaCl, is mixed with a well solution containing 0.17 M sodium acetate, pH 6.5, 85 mM sodium cacodylate, 50% w/v PEG 8000, and 15% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution using single anomalous dispersion or trimethyl lead(IV) acetate derivatives	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant detagged isolated S1 domain, residues 35-125, large crystals grow within 4 weeks in 1.65 mM protein containing solution of 20 mM phosphate, pH 6.5, 50 mM NaCl, and 0.05% w/v NaN3 at 4°C, isomorphous crystals are grown by hanging drop vapour diffusion method at 18°C, 1.3 mM protein in 20 mM HEPES, p 6.5, 50 mM NaCl, is mixed with a well solution containing 0.17 M sodium acetate, pH 6.5, 85 mM sodium cacodylate, 50% w/v PEG 8000, and 15% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution using single anomalous dispersion or trimethyl lead(IV) acetate derivatives

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
G66S	site-directed mutagenesis, the mutation leads to a dramatic destabilization of the OB fold of the S1 domain and leads to increased temperature sensitivity of the mutant compared to the wild-type enzyme	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P21513	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally His6-tagged wild-type and mutant full-length enzymes, and isolated N-terminally His6-tagged S1 domain by nickel affinity chromatography, removal of the His-tags by thrombin	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	nucleic acid binding structure, structure-function relationship, overview	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
More	structural characterization of the RNase E S1 domain, residues 25-125, by NMR, and identification of its oligonucleotide-binding and dimerization interfaces, overview, isolated S1 domain, which shows an OB fold, undergoes a specific monomer-dimer equilibrium in solution with a KD in the millimolar range	Escherichia coli
tetramer	dimer composed of two dimers, tertiary and quarternary structure, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
RNase E	-	Escherichia coli