Molecular dynamics of ribosomal elongation factors G and Tu
作者： Katarzyna Kulczycka , Maciej Długosz , Joanna Trylska
DOI: 10.1007/S00249-010-0647-2
关键词:
摘要: Translation on the ribosome is controlled by external factors. During polypeptide lengthening, elongation factors EF-Tu and EF-G consecutively interact with bacterial ribosome. binds delivers an aminoacyl-tRNA to ribosomal A site helps translocate tRNAs between their binding sites after peptide bond formed. These processes occur at expense of GTP. EF-Tu:tRNA are similar shape, share a common site, undergo large conformational changes interaction To characterize internal motion these two factors, we used 25 ns long all-atom molecular dynamics simulations. We observed enhanced mobility domains III, IV, V tRNA in complex. EF-Tu:GDP complex acquired configuration different from that found crystal structure GTP analogue, showing switch I II regions. The calculated electrostatic properties showed no global similarity even though matching surface patches were around domain contacts ribosome, GDP/GTP region.
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