Abdulkarim F, Liljas L, Hughes D
Department of Molecular Biology, Uppsala University, Sweden.
FEBS Lett. 1994 Sep 26;352(2):118-22. doi: 10.1016/0014-5793(94)00937-6.
The antibiotic kirromycin inhibits protein synthesis by binding to EF-Tu and preventing its release from the ribosome after GTP hydrolysis. We have isolated and sequenced a collection of kirromycin resistant tuf mutations and identified thirteen single amino acid substitutions at seven different sites in EF-Tu. These have been mapped onto the 3D structures of EF-Tu.GTP and EF-Tu.GDP. In the active GTP form of EF-Tu the mutations cluster on each side of the interface between domains I and III. We propose that this domain interface is the binding site for kirromycin.
抗生素奇霉素通过与EF-Tu结合并在GTP水解后阻止其从核糖体释放来抑制蛋白质合成。我们分离并测序了一组奇霉素抗性tuf突变体，并在EF-Tu的七个不同位点鉴定出13个单氨基酸取代。这些突变已定位到EF-Tu.GTP和EF-Tu.GDP的三维结构上。在EF-Tu的活性GTP形式中，突变聚集在结构域I和III之间界面的两侧。我们认为这个结构域界面是奇霉素的结合位点。
