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Crystal structure at 1.2 Å 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 Å resolution. It indicates a single α/β globular domain built around a twisted mixed β‐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.