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5.4.99.21: 23S rRNA pseudouridine2604 synthase

This is an abbreviated version!
For detailed information about 23S rRNA pseudouridine2604 synthase, go to the full flat file.

Reaction

23S rRNA uridine2604
=
23S rRNA pseudouridine2604

Synonyms

RluF, YjbC

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.21 23S rRNA pseudouridine2604 synthase

Crystallization

Crystallization on EC 5.4.99.21 - 23S rRNA pseudouridine2604 synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging-drop vapor-diffusion method, domain architecture and crystal structure of the catalytic domain of RluF at 2.6 A resolution. Limited proteolysis, mass spectrometry and N-terminal sequencing indicate that RluF has a distinct domain architecture, with the catalytic domain flanked at the N and C termini by additional domains connected to it by flexible linkers. The structure of the catalytic domain of RluF is similar to those of RsuA and TruB. Structural comparison of RluF with its closest structural homologues, RsuA and TruB, suggests possible functional roles for the N-terminal and C-terminal domains of RluF
hanging-drop vapor-diffusion method, X-ray crystal structure of RluF bound to the isolated stem–loop, in which uridine2604 is substituted by 5-fluorouridine to prevent catalytic turnover