1ze1

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Revision as of 08:17, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1ze1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ze1, resolution 2.9Å" /> '''Conformational Change...)
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File:1ze1.gif


1ze1, resolution 2.9Å

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Conformational Change of Pseudouridine 55 Synthase upon Its Association with RNA Substrate

OverviewOverview

Pseudouridine 55 synthase (Psi55S) catalyzes isomerization of uridine (U), to pseudouridine (Psi) at position 55 in transfer RNA. The crystal, structures of Thermotoga maritima Psi55S, and its complex with RNA, have, been determined at 2.9 and 3.0 A resolutions, respectively. Structural, comparisons with other families of pseudouridine synthases (PsiS) indicate, that Psi55S may acquire its ability to recognize a stem-loop RNA substrate, by two insertions of polypeptides into the PsiS core. The structure of, apo-Psi55S 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.

About this StructureAbout this Structure

1ZE1 is a Single protein structure of sequence from Thermotoga maritima with MG as ligand. Active as Pseudouridylate synthase, with EC number 4.2.1.70 Full crystallographic information is available from OCA.

ReferenceReference

Conformational change of pseudouridine 55 synthase upon its association with RNA substrate., Phannachet K, Huang RH, Nucleic Acids Res. 2004 Feb 27;32(4):1422-9. Print 2004. PMID:14990747

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