Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase |
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Authors: | Grimm Clemens Ficner Ralf Sgraja Tanja Haebel Peter Klebe Gerhard Reuter Klaus |
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Affiliation: | Institut für Pharmazeutische Chemie, Philipps-Universit?t Marburg, Marbacher Weg 6, 35032 Marburg, Germany. |
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Abstract: | 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. |
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Keywords: | QueA tRNA modification S-adenosylmethionine Queuosine Queuine |
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