2pth

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{{STRUCTURE_2pth| PDB=2pth | SCENE= }}
{{STRUCTURE_2pth| PDB=2pth | SCENE= }}
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'''PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI'''
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===PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9303320}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Peptidyl-trna]]
[[Category: Peptidyl-trna]]
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Revision as of 13:03, 29 July 2008

Template:STRUCTURE 2pth

PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 9303320

About this Structure

2PTH is a Single protein structure of sequence from Escherichia coli. 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

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