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

被引：27

作者：

Ericsson, UB ^{[1
]}

Nordlund, P ^{[1
]}

Hallberg, BM ^{[1
]}

机构：

[1] Stockholm Univ, Dept Biochem & Biophys, SE-11421 Stockholm, Sweden

来源：

FEBS LETTERS | 2004年 / 565卷 / 1-3期

关键词：

pseudouridine synthase; RNA modification; tRNA; TruD; Pus7;

D O I：

10.1016/j.febslet.2004.03.085

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：59 / 64

页数：6

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