Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold

J Biol Chem. 2004 Apr 30;279(18):18107-10. doi: 10.1074/jbc.C400072200. Epub 2004 Mar 3.


TruD, a recently discovered novel pseudouridine synthase in Escherichia coli, is responsible for modifying uridine13 in tRNA(Glu) 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 alpha/beta fold that up to now has not been found in any other protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Catalytic Domain
  • Crystallography, X-Ray*
  • Escherichia coli Proteins / chemistry
  • Hydro-Lyases / chemistry*
  • Protein Conformation
  • Sequence Alignment
  • Structural Homology, Protein


  • Escherichia coli Proteins
  • Hydro-Lyases
  • pseudouridylate synthetase

Associated data

  • PDB/1SI7