PheRS belongs to class IIc and is a tetrameric enzyme consisting of two alphabeta heterodimers. The B3/4 domain of the beta-subunit catalyzes the editing, domain architecture, overview
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit, 0.001 ml of protein solution containing 36 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl, mixed with 0.001 ml of precipitant solution, containing 100 mM sodium citrate, pH 5.6, and 16.5% PEG 20000, covarage with a 1:1 mixture of paraffin oil and silicone, 20°C, 1 week, soaking in a soaked in a cryoprotectant solution containing 100 mM sodium citrate, pH 5.6, 18.2% PEG 20000, and 20% glycerol, X-ray diffraction structure determination and analysis at 1.94 A resolution
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain B834(DE3) by anion exchange chromatography, adsorption chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain BL21(DE3), expression of selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain B834(DE3)
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ped-IYRS, overview