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Literature summary for 5.4.99.23 extracted from

  • Mizutani, K.; Machida, Y.; Unzai, S.; Park, S.Y.; Tame, J.R.
    Crystal structures of the catalytic domains of pseudouridine synthases RluC and RluD from Escherichia coli (2004), Biochemistry, 43, 4454-4463.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
23S rRNA uridine1911/uridine1915/uridine1917 Escherichia coli
-
23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P33643
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
23S rRNA uridine1911/uridine1915/uridine1917
-
Escherichia coli 23S rRNA pseudouridine1911/pseudouridine1915/pseudouridine1917
-
?

Subunits

Subunits Comment Organism
monomer analytical ultracentrifugation sedimentation velocity experiments show that RluD is monomeric in solution Escherichia coli

Synonyms

Synonyms Comment Organism
pseudouridine synthases RluD
-
Escherichia coli
RluD
-
Escherichia coli