Crystal structure at 1.2 angstrom resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase

Peptidyl-tRNA hydrolase activity from Escherichia coli ensures the recycling of peptidyl-tRNAs produced through abortion of translation, This activity, which is essential for cell viability, is carried out by a monomeric protein of 193 residues, The structure of crystalline peptidyl-tRNA hydrolase could be solved at 1.2 Angstrom resolution, It indicates a single alpha/beta globular domain built around a twisted mixed beta-sheet, similar to the central core of an aminopeptidase from Aeromonas proteolytica, This similarity allowed the characterization by site-directed mutagenesis of several residues of the active site of peptidyl-tRNA hydrolase, These residues, strictly conserved among the known peptidyl-tRNA hydrolase sequences, delineate a channel which, in the crystal, is occupied by the C-end of a neighbouring peptidyl-tRNA hydrolase molecule, Hence, several main chain atoms of three residues belonging to one peptidyl-tRNA hydrolase polypeptide establish contacts inside the active site of another peptidyl-tRNA hydrolase molecule, Such an interaction is assumed to represent the formation of a complex between the enzyme and one product of the catalysed reaction.