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Conformational change of pseudouridine 55 synthase upon its association with RNA substrate

By Kulwadee Phannachet and Raven H. Huang

Abstract

Pseudouridine 55 synthase (Ψ55S) catalyzes isomerization of uridine (U) to pseudouridine (Ψ) at position 55 in transfer RNA. The crystal structures of Thermotoga maritima Ψ55S, and its complex with RNA, have been determined at 2.9 and 3.0 Å resolutions, respectively. Structural comparisons with other families of pseudouridine synthases (ΨS) indicate that Ψ55S may acquire its ability to recognize a stem–loop RNA substrate by two insertions of polypeptides into the ΨS core. The structure of apo-Ψ55S reveals that these two insertions interact with each other. However, association with RNA substrate induces substantial conformational change in one of the insertions, resulting in disruption of interaction between insertions and association of both insertions with the RNA substrate. Specific interactions between two insertions, as well as between the insertions and the RNA substrate, account for the molecular basis of the conformational change

Topics: Articles
Publisher: Oxford University Press
Year: 2004
DOI identifier: 10.1093/nar/gkh287
OAI identifier: oai:pubmedcentral.nih.gov:390278
Provided by: PubMed Central
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