Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone

Three crystal structures of the prolyl-tRNA synthetase domain of human glutamyl-prolyl-tRNA synthetase, two of which were complexed with small molecules, were determined by Zn-SAD phasing combined with molecular replacement. The structures revealed that conformational changes occur in the active site upon small-molecule binding.

Protein design by fusion: implications for protein structure prediction and evolution

The design of a new protein fold by fusion of a heterodimer is described.