BRENDA - Enzyme Database

Crystal structures of the catalytic domains of pseudouridine synthases RluC and RluD from Escherichia coli

Mizutani, K.; Machida, Y.; Unzai, S.; Park, S.Y.; Tame, J.R.; Biochemistry 43, 4454-4463 (2004)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
5.4.99.23
-
Escherichia coli
5.4.99.24
-
Escherichia coli
Crystallization (Commentary)
EC Number
Crystallization
Organism
5.4.99.23
crystals of full-length RluD are grown at 20C 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
Escherichia coli
5.4.99.24
crystals of the catalytic domain RluC(92-319) are grown at 20C using the hanging drop method
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5.4.99.23
23S rRNA uridine1911/uridine1915/uridine1917
Escherichia coli
-
23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
-
-
?
5.4.99.24
23S rRNA uridine955/uridine2504/uridine2580
Escherichia coli
-
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.4.99.23
Escherichia coli
P33643
-
-
5.4.99.24
Escherichia coli
P0AA39
-
-
Purification (Commentary)
EC Number
Commentary
Organism
5.4.99.23
-
Escherichia coli
5.4.99.24
-
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.23
23S rRNA uridine1911/uridine1915/uridine1917
-
702207
Escherichia coli
23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
-
-
-
?
5.4.99.24
23S rRNA uridine955/uridine2504/uridine2580
-
702207
Escherichia coli
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
5.4.99.23
monomer
analytical ultracentrifugation sedimentation velocity experiments show that RluD is monomeric in solution
Escherichia coli
5.4.99.24
monomer
analytical ultracentrifugation sedimentation velocity experiments show that RluC(92-319) is monomeric in solution
Escherichia coli
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
5.4.99.23
-
Escherichia coli
5.4.99.24
-
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
5.4.99.23
crystals of full-length RluD are grown at 20C 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
Escherichia coli
5.4.99.24
crystals of the catalytic domain RluC(92-319) are grown at 20C using the hanging drop method
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5.4.99.23
23S rRNA uridine1911/uridine1915/uridine1917
Escherichia coli
-
23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
-
-
?
5.4.99.24
23S rRNA uridine955/uridine2504/uridine2580
Escherichia coli
-
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
5.4.99.23
-
Escherichia coli
5.4.99.24
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.23
23S rRNA uridine1911/uridine1915/uridine1917
-
702207
Escherichia coli
23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
-
-
-
?
5.4.99.24
23S rRNA uridine955/uridine2504/uridine2580
-
702207
Escherichia coli
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
5.4.99.23
monomer
analytical ultracentrifugation sedimentation velocity experiments show that RluD is monomeric in solution
Escherichia coli
5.4.99.24
monomer
analytical ultracentrifugation sedimentation velocity experiments show that RluC(92-319) is monomeric in solution
Escherichia coli