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

Ericsson UB, Nordlund P, Hallberg BM



Published 2004-05-07 in FEBS Lett volume 565 .

Pubmed ID: 15135053
DOI identifier: -

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.


This publication refers to following proteins:



Entry added on: 2011-10-17 10:38:48.760010, by a user: magda