Crystal Structure of TruD, a Novel Pseudouridine Synthase with a New Protein Fold

Yusuf Kaya, Mark Del Campo, James Ofengand, Arun Malhotra

Research output: Contribution to journalArticle

32 Scopus citations


TruD, a recently discovered novel pseudouridine synthase in Escherichia coli, is responsible for modifying uridine13 in tRNAGGlu to pseudouridine. It has little sequence homology with the other 10 pseudouridine synthases in E. coli which themselves have been grouped into four related protein families. Crystal structure determination of TruD revealed a two domain structure consisting of a catalytic domain that differs in sequence but is structurally very similar to the catalytic domain of other pseudouridine synthases and a second large domain (149 amino acids, 43% of total) with a novel α/β fold that up to now has not been found in any other protein.

Original languageEnglish (US)
Pages (from-to)18107-18110
Number of pages4
JournalJournal of Biological Chemistry
Issue number18
StatePublished - Apr 30 2004


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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