CRYSTAL STRUCTURE OF METHIONYL-TRNA SYNTHETASE COMPLEXED WITH TRNA

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Aminoacyl-tRNA synthetases catalyze the attachment of amino acid to cognate tRNA as the first step in protein biosynthesis. Aminoacylation must be specific and efficient for protein synthesis to be both fast and accurate. Based on the known conformational changes that occur in protein-RNA complexes in general and aminoacyl-tRNA complexes in particular, we hypothesize that efficient catalysis by methionyl-tRNA synthetase (MetRS) requires conformational rearrangements of both tRNA and MetRS, induced by cognate anticodon binding. This proposed mutually induced fit of the tRNA and MetRS probably drives long-range communication between the anticodon-binding site in the C-terminal domain of MetRS and the catalytic active site of the enzyme, located approximately 75 ? away. To visualize the conformational change and the inter-domain communication upon tRNA binding to MetRS, we are pursuing to determine the crystal structure of the E. coli MetRS:tRNA complex.