Information on EC 5.4.99.21 - 23S rRNA pseudouridine2604 synthase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
5.4.99.21
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RECOMMENDED NAME
GeneOntology No.
23S rRNA pseudouridine2604 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
23S rRNA uridine2604 = 23S rRNA pseudouridine2604
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
23S rRNA-uridine2604 uracil mutase
The enzyme is not completely specific for uridine2604 and can, to a small extent, also react with uridine2605 [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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pseudouridine2604 is absent in the RluF-deletion strain
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
23S rRNA uridine2604
23S rRNA pseudouridine2604
show the reaction diagram
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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
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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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
full-length RluF and N-terminal, 65-residue-truncated RulF (DELTARulF)
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using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D107N
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inactive mutant enzyme
D107T
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inactive mutant enzyme
Show AA Sequence (114 entries)
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