2pth
From Proteopedia
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PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI
Overview
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.
About this Structure
2PTH is a Single protein structure of sequence from Escherichia coli. Active as Aminoacyl-tRNA hydrolase, with EC number 3.1.1.29 Full crystallographic information is available from OCA.
Reference
Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase., Schmitt E, Mechulam Y, Fromant M, Plateau P, Blanquet S, EMBO J. 1997 Aug 1;16(15):4760-9. PMID:9303320
Page seeded by OCA on Wed Nov 21 13:39:39 2007
