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 Citations (Scopus)

Abstract

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
Pages (from-to)18107-18110
Number of pages4
JournalJournal of Biological Chemistry
Volume279
Issue number18
DOIs
StatePublished - Apr 30 2004

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Crystal structure
Escherichia coli
Catalytic Domain
Pseudouridine
Proteins
Sequence Homology
Amino Acids
pseudouridine synthases

ASJC Scopus subject areas

  • Biochemistry

Cite this

Crystal Structure of TruD, a Novel Pseudouridine Synthase with a New Protein Fold. / Kaya, Yusuf; Del Campo, Mark; Ofengand, James; Malhotra, Arun.

In: Journal of Biological Chemistry, Vol. 279, No. 18, 30.04.2004, p. 18107-18110.

Research output: Contribution to journalArticle

Kaya, Yusuf ; Del Campo, Mark ; Ofengand, James ; Malhotra, Arun. / Crystal Structure of TruD, a Novel Pseudouridine Synthase with a New Protein Fold. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 18. pp. 18107-18110.
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