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X‐ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold
Author(s) -
Ericsson Ulrika B.,
Nordlund Pär,
Hallberg B.Martin
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.03.085
Subject(s) - pseudouridine , transfer rna , rna , chemistry , uridine , escherichia coli , atp synthase , stereochemistry , biochemistry , biology , enzyme , gene
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 Å 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.