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FEBS Lett. 2004 May 7;565(1-3):59-64.

X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold.

Author information

1
Department of Biochemistry and Biophysics, Stockholm University, Roslagstullsbacken 15, SE-114 21 Stockholm, Sweden.

Abstract

Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine in structural RNA. The pseudouridine synthase TruD, that modifies U13 in tRNA, belongs to a recently identified and large family of pseudouridine synthases present in all kingdoms of life. We report here the crystal structure of Escherichia coli TruD at 2.0 A resolution. The structure reveals an overall V-shaped molecule with an RNA-binding cleft formed between two domains: a catalytic domain and an insertion domain. The catalytic domain has a fold similar to that of the catalytic domains of previously characterised pseudouridine synthases, whereas the insertion domain displays a novel fold.

PMID:
15135053
DOI:
10.1016/j.febslet.2004.03.085
[Indexed for MEDLINE]
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