Ericsson Ulrika B, Nordlund Pär, Hallberg B Martin
Department of Biochemistry and Biophysics, Stockholm University, Roslagstullsbacken 15, SE-114 21 Stockholm, Sweden.
FEBS Lett. 2004 May 7;565(1-3):59-64. doi: 10.1016/j.febslet.2004.03.085.
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.
假尿苷合酶催化结构RNA中尿苷异构化为假尿苷。修饰tRNA中U13的假尿苷合酶TruD属于最近鉴定出的、存在于所有生命王国中的一个庞大的假尿苷合酶家族。我们在此报告大肠杆菌TruD在2.0埃分辨率下的晶体结构。该结构揭示了一个整体呈V形的分子，在两个结构域之间形成了一个RNA结合裂隙：一个催化结构域和一个插入结构域。催化结构域的折叠与先前表征的假尿苷合酶的催化结构域相似，而插入结构域则呈现出一种新颖的折叠方式。
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