3.1.26.12: ribonuclease E
This is an abbreviated version!
For detailed information about ribonuclease E, go to the full flat file.
Word Map on EC 3.1.26.12
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3.1.26.12
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degradosome
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polynucleotide
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phosphorylase
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pnpase
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srnas
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endonuclease
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hfq
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helicase
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endonucleolytic
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exoribonuclease
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single-stranded
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enolase
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stem-loops
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polya
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rna-binding
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polycistronic
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ribonucleolytic
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e-dependent
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base-pairing
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dead-box
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autoregulation
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e-mediated
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e-like
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ompa
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endoribonucleolytic
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5'-terminal
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intercistronic
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cole1-type
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monophosphorylated
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5'-monophosphorylated
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shine-dalgarno
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rho-independent
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hfq-dependent
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glucosamine-6-phosphate
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riboswitches
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au-rich
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glm
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rna-processing
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crescentus
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analysis
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medicine
- 3.1.26.12
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degradosome
- polynucleotide
- phosphorylase
- pnpase
- srnas
- endonuclease
- hfq
- helicase
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endonucleolytic
- exoribonuclease
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single-stranded
- enolase
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stem-loops
- polya
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rna-binding
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polycistronic
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ribonucleolytic
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e-dependent
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base-pairing
-
dead-box
-
autoregulation
-
e-mediated
-
e-like
- ompa
-
endoribonucleolytic
-
5'-terminal
-
intercistronic
-
cole1-type
-
monophosphorylated
-
5'-monophosphorylated
-
shine-dalgarno
-
rho-independent
-
hfq-dependent
- glucosamine-6-phosphate
- riboswitches
-
au-rich
- glm
-
rna-processing
- crescentus
- analysis
- medicine
Reaction
endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions =
Synonyms
Ams/Rne/Hmp1 polypeptide, AqaRng, endoribonuclease E, endoribonuclease RNase E, More, NCgl2281, ribonuclease E, RNase E, RNase E/G, RNase E/G-type endoribonuclease, RNase ES, RNase EV, RNaseE, Rne, Rne protein, RneC, Rng, SSO1404, SynRne
ECTree
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Crystallization
Crystallization on EC 3.1.26.12 - ribonuclease E
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apoprotein, X-ray diffraction structure determination and analysis at 3.3 resolution, modelling using molecular replacement
crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage
enolase bound to its cognate site from RNase E, residues 823-850, X-ray diffraction structure determination and analysis at 1.9 A resolution
PNPase complexed with the recognition site from RNase E and with manganese in the presence or in the absence of modified RNA, hanging drop vapour diffusion method, using 0.2 M ammonium nitrate and 20% w/v PEG 3350 or 0.2 M diammonium hydrogen citrate and 17% PEG 3350
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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
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
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the crystal structure of enolase bound to its cognate site from RNase E, residues 823-850, at 1.9 A resolution. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E
X-ray diffraction structure determination and analysis at 2.9 A resolution
hanging drop vapor diffusion method. The crystal structure of SSO1404 is solved at 1.6 A resolution revealing the first ribonuclease with a ferredoxin-like fold