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Literature summary for 5.4.99.12 extracted from

  • Foster, P.G.; Huang, L.; Santi, D.; Stroud, R.
    The structural basis of tRNA recognition and pseudouridine formation by pseudouridine synthase I (2000), Nat. Struct. Biol., 7, 23-27.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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Escherichia coli
native protein, to 1.5 A resolution, and several derivatives. Structure reveals a dimeric protein that contains two positively charged, RNA-binding clefts along the surface of the protein. Each cleft contains a highly conserved aspartic acid located at its center. The structure suggests that a dimeric enzyme is required for binding transfer RNA and subsequent pseudouridine formation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Subunits

Subunits Comment Organism
dimer
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Escherichia coli
dimer crystallization data Escherichia coli

Synonyms

Synonyms Comment Organism
pseudouridine synthase I
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Escherichia coli