PMID:15135053

Citation	Ericsson, UB, Nordlund, P and Hallberg, BM (2004) X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold. FEBS Lett. 565:59-64
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.
Links	PubMed Online version:10.1016/j.febslet.2004.03.085
Keywords	Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Electrons; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Intramolecular Transferases/chemistry; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Folding; Protein Structure, Tertiary; RNA, Transfer/chemistry; Saccharomyces cerevisiae Proteins/chemistry; Sequence Homology, Amino Acid
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