2PTH

PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI

Summary for 2PTH

• Entry DOI: 10.2210/pdb2pth/pdb
• Descriptor: PEPTIDYL-TRNA HYDROLASE (2 entities in total)
• Functional Keywords: hydrolase, peptidyl-trna
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A7D1
• Total number of polymer chains: 1
• Total formula weight: 20982.12

Authors

Schmitt, E.,Mechulam, Y.,Fromant, M.,Plateau, P.,Blanquet, S. (deposition date: 1997-03-25, release date: 1998-03-25, Last modification date: 2024-02-21)

Primary citation

Schmitt, E.,Mechulam, Y.,Fromant, M.,Plateau, P.,Blanquet, S.
Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase.
EMBO J., 16:4760-4769, 1997

PubMed Abstract: 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 A 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.

PubMed: 9303320
DOI: 10.1093/emboj/16.15.4760

Experimental method

X-RAY DIFFRACTION (1.2 Å)