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Literature summary for 5.4.99.21 extracted from

  • Czudnochowski, N.; Ashley, G.W.; Santi, D.V.; Alian, A.; Finer-Moore, J.; Stroud, R.M.
    The mechanism of pseudouridine synthases from a covalent complex with RNA, and alternate specificity for U2605 versus U2604 between close homologs (2014), Nucleic Acids Res., 42, 2037-2048.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of Escherichia coli RluF in a complex with a 22-mer RNA substrate analog identical in sequence to the substrate rRNA stem-loop, except with the target U2604 substituted by 5-fluorouridine to block a late step in catalysis. The structure shows that association with RluF induces a rearrangement of the RNA stem-loop, resulting in a frame-shift in base pairing. A bulge in the RNA is induced to fold into the stem, causing the RNA 3' to the bulge to translate by 1nt, thereby flipping out U2604 into the active site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P32684
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-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Escherichia coli

Synonyms

Synonyms Comment Organism
RluF
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Escherichia coli