1yy3
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(New page: 200px<br /><applet load="1yy3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yy3, resolution 2.88Å" /> '''Structure of S-Adeno...)
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Revision as of 05:00, 21 November 2007
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Structure of S-Adenosylmethionine:tRNA Ribosyltransferase-Isomerase (QueA)
Overview
The enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA), is involved in the biosynthesis of the hypermodified tRNA nucleoside, queuosine. It is unprecedented in nature as it uses the cofactor, S-adenosylmethionine as the donor of a ribosyl group. We have determined, the crystal structure of Bacillus subtilis QueA at a resolution of 2.9A., The structure reveals two domains representing a 6-stranded beta-barrel, and an alpha beta alpha-sandwich, respectively. All amino acid residues, invariant in the QueA enzymes of known sequence cluster at the interface, of the two domains indicating the localization of the substrate binding, region and active center. Comparison of the B. subtilis QueA structure, with the structure of QueA from Thermotoga maritima suggests a high domain, flexibility of this enzyme.
About this Structure
1YY3 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase., Grimm C, Ficner R, Sgraja T, Haebel P, Klebe G, Reuter K, Biochem Biophys Res Commun. 2006 Dec 22;351(3):695-701. Epub 2006 Oct 30. PMID:17083917
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