Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.12 extracted from

  • Koslover, D.J.; Callaghan, A.J.; Marcaida, M.J.; Garman, E.F.; Martick, M.; Scott, W.G.; Luisi, B.F.
    The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation (2008), Structure, 16, 1238-1244.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
apoprotein, X-ray diffraction structure determination and analysis at 3.3 resolution, modelling using molecular replacement Escherichia coli
RNase E catalytic domain in the apo-state, molecular replacement Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the magnesium ion is co-recruited with RNA during ligand binding Escherichia coli
Zn2+ conformation and activity of apo- and holoenzyme, modelling, overview Escherichia coli
Zn2+ the enzyme contains Zn2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P21513
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview Escherichia coli ?
-
?
additional information RNA degradation mechanism, overview Escherichia coli ?
-
?
additional information RNase E preferres substrates possessing a 5'-monophosphate Escherichia coli ?
-
?
additional information upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site Escherichia coli ?
-
?
mRNA + H2O
-
Escherichia coli ?
-
?
tRNAPhe precursor + H2O
-
Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer dimer of dimers, RNase E apoprotein, X-ray crystallography Escherichia coli
tetramer a pair of dimers, the quaternary organization of RNase E is flexible, modelling, apoprotein formation leads to a conformational change in which the 5' sensor and S1 subdomains move as a single unit through an angle between the apoprotein and holoprotein state, overview Escherichia coli
tetramer RNase E holoenzyme, X-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
RNase E
-
Escherichia coli