Dynamics of Recognition between tRNA and elongation factor Tu.

ABSTRACT: Elongation factor Tu (EF-Tu) binds to all standard aminoacyl transfer RNAs (aa-tRNAs) and transports them to the ribosome while protecting the ester linkage between the tRNA and its cognate amino acid. We use molecular dynamics simulations to investigate the dynamics of the EF-Tu.guanosine 5'-triphosphate.aa-tRNA(Cys) complex and the roles played by Mg2+ ions and modified nucleosides on the free energy of protein.RNA binding. Individual modified nucleosides have pronounced effects on the structural dynamics of tRNA and the EF-Tu.Cys-tRNA(Cys) interface. Combined energetic and evolutionary analyses identify the coevolution of residues in EF-Tu and aa-tRNAs at the binding interface. Highly conserved EF-Tu residues are responsible for both attracting aa-tRNAs as well as providing nearby nonbo

SUBMITTER: Eargle J 

PROVIDER: S-EPMC3232051 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature