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Literature summary for 5.4.99.24 extracted from

  • Corollo, D.; Blair-Johnson, M.; Conrad, J.; Friedler, T.; Sun, D.; Wang, L.; Ofengand, J.; Fenna, R.
    Crystallisation and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli (1999), Acta Crystallogr. Sect. D, 55, 302-304.
No PubMed abstract available
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
additional information a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AA39
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
23S rRNA uridine955/uridine2504/uridine2580
-
 Escherichia coli 23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
 ?

Synonyms

Synonyms Comment Organism
RLuc
-
 Escherichia coli