Information on EC 5.4.99.23 - 23S rRNA pseudouridine1911/1915/1917 synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.4.99.23
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RECOMMENDED NAME
GeneOntology No.
23S rRNA pseudouridine1911/1915/1917 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
23S rRNA uridine1911/uridine1915/uridine1917 = 23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
23S rRNA-uridine1911/1915/1917 uracil mutase
Pseudouridine synthase RluD converts uridines at positions 1911, 1915, and 1917 of 23S rRNA to pseudouridines. These nucleotides are located in the functionally important helix-loop 69 of 23S rRNA [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the structure of RluD (a RluA family member) emphasizes that the RluA, RsuA, TruB, and TruA families of pseudouridine synthases arose by divergent evolution from a common ancestor
malfunction
physiological function
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 uridine1911/uridine1915/uridine1917
23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
23S rRNA uridine1911/uridine1915/uridine1917
23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
show the reaction diagram
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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x * 44000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 44000, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.0 A structure of the catalytic domain of RluD (residues 77–326). The catalytic domain folds into a mainly antiparallel beta-sheet flanked by several loops and helices. A positively charged cleft that presumably binds RNA leads to the conserved Asp139. The RluD N-terminal S4 domain, connected by a flexible linker, is disordered in our structure. RluD is very similar in both catalytic domain structure and active site arrangement to the pseudouridine synthases RsuA, TruB, and TruA
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crystallization of selenomethionine-substituted RluD by the hanging-drop method, crystals diffract to 1.9 A and belong to space group P4(3)2(1)2, with unit cell parameters a = b = 75.14, c = 181.81 A
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crystals of full-length RluD are grown at 20°C using the hanging drop method. The S4 domain of RluD appears to be highly flexible or unfolded and is completely invisible in the electron density map
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crystals of SeMet-labeled DELTARluD are obtained under oil by the microbatch method, crystal structure of the catalytic module of RluD (residues 68–326, DELTARluD) refined at 1.8 A to a final R-factor of 21.8%. DELTARluD is a monomeric enzyme having an overall mixed alpha/beta fold. The DELTARluD molecule consists of two subdomains, a catalytic subdomain and C-terminal subdomain with the RNA-binding cleft formed by loops extending from the catalytic sub-domain. Comparison of the structure with other pseudouridine synthases
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli
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wild-type and mutant enzymes D139T and D139N are overexpressed from plasmids
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D139N
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mutation completely blocks pseudouridine formation in vivo and in vitro. The mutant rluD gene produces a protein capable of complete reversal of the growth defect (of Escherichia coli mutant with a truncation in the rluD gene) without concomitant pseudouridine formation
D139T
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mutation completely blocks pseudouridine formation in vivo and in vitro. The mutant rluD gene produces a protein capable of complete reversal of the growth defect (of Escherichia coli mutant with a truncation in the rluD gene) without concomitant pseudouridine formation
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