BRENDA - Enzyme Database

Crystallisation and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli

Corollo, D.; Blair-Johnson, M.; Conrad, J.; Friedler, T.; Sun, D.; Wang, L.; Ofengand, J.; Fenna, R.; Acta Crystallogr. Sect. D 55, 302-304 (1999)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
4.2.1.70
RluC, expression in Escherichia coli
Escherichia coli
5.4.99.24
-
Escherichia coli
Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.70
pseudouridine synthase RluC fragment
Escherichia coli
5.4.99.24
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity. Crystals of this fragment, grown by precipitation with sodium acetate at pH 8.0, belong to space group P321, with unit-cell dimensions a = b = 97.1, c = 86.3 A and have two molecules in the crystallographic asymmetric unit. Crystals diffract X-rays to at least 2.3 A resolution and appear suitable for crystal structure determination
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
5.4.99.24
additional information
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity
Escherichia coli
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.70
Escherichia coli
-
-
-
5.4.99.24
Escherichia coli
P0AA39
-
-
Purification (Commentary)
EC Number
Commentary
Organism
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
5.4.99.24
23S rRNA uridine955/uridine2504/uridine2580
-
5857
Escherichia coli
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
-
?
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.70
RluC, expression in Escherichia coli
Escherichia coli
5.4.99.24
-
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.70
pseudouridine synthase RluC fragment
Escherichia coli
5.4.99.24
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity. Crystals of this fragment, grown by precipitation with sodium acetate at pH 8.0, belong to space group P321, with unit-cell dimensions a = b = 97.1, c = 86.3 A and have two molecules in the crystallographic asymmetric unit. Crystals diffract X-rays to at least 2.3 A resolution and appear suitable for crystal structure determination
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
5.4.99.24
additional information
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity
Escherichia coli
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
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
5.4.99.24
23S rRNA uridine955/uridine2504/uridine2580
-
5857
Escherichia coli
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
-
?