Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase
| Autor: | Clemens Grimm, Gerhard Klebe, Klaus Reuter, Tanja Sgraja, Peter W. Haebel, Ralf Ficner |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular TRNA modification Protein Conformation Molecular Sequence Data Biophysics Queuosine Bacillus subtilis Isomerase Biochemistry Cofactor Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Computer Simulation Amino Acid Sequence Isomerases Molecular Biology 030304 developmental biology 0303 health sciences Binding Sites Crystallography biology 030302 biochemistry & molecular biology Queuine Cell Biology biology.organism_classification Protein Structure Tertiary Enzyme Activation Models Chemical chemistry Thermotoga maritima Transfer RNA biology.protein Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 351:695-701 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2006.10.096 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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