Journal: The EMBO Journal
Article Title: The structure of an AspRS-tRNAAsp complex reveals a tRNA-dependent control mechanism
Figure Lengend Snippet: Fig. 5. ( A ) Stereoview of the active site area of E.coli AspRS with bound yeast tRNA Asp and aspartyl-adenylate. The (2 F o – F c ) electron density map contoured at 1σ shows the aspartyl-adenylate substrate sitting on the antiparallel β-sheet of the catalytic domain. The flipping loop (residues 167–174 colored in blue) adopts a closed conformation. The contribution of this loop is essential to the binding of the aspartyl-adenylate and tRNA terminal adenosine substrates. (B–D) Conformation of the flipping loop and the tRNA terminal adenosine in ( B ) the yeast AspRS–yeast tRNA Asp complex, ( C ) the heterologous E.coli AspRS–yeast tRNA Asp complex and ( D ) the E.coli AspRS– E.coli tRNA Asp complex. The aspartyl-adenylate substrate is present in all three complexes.
Article Snippet: Coordinates for the X-ray structure of the E.coli AspRS–yeast tRNAAsp –aspartyl-adenylate have been deposited in the Brookhaven Protein Data Bank under accession code 1IL2.
Techniques: Binding Assay