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
UNIPROT
ORGANISM
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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