2pth: Difference between revisions

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[[Image:2pth.jpg|left|200px]]
[[Image:2pth.jpg|left|200px]]


{{Structure
<!--
|PDB= 2pth |SIZE=350|CAPTION= <scene name='initialview01'>2pth</scene>, resolution 1.2&Aring;
The line below this paragraph, containing "STRUCTURE_2pth", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] </span>
or leave the SCENE parameter empty for the default display.
|GENE= PTH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
-->
|DOMAIN=
{{STRUCTURE_2pth|  PDB=2pth |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pth OCA], [http://www.ebi.ac.uk/pdbsum/2pth PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pth RCSB]</span>
}}


'''PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI'''
'''PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI'''
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[[Category: Plateau, P.]]
[[Category: Plateau, P.]]
[[Category: Schmitt, E.]]
[[Category: Schmitt, E.]]
[[Category: hydrolase]]
[[Category: Hydrolase]]
[[Category: peptidyl-trna]]
[[Category: Peptidyl-trna]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:46:45 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:40:28 2008''

Revision as of 10:46, 4 May 2008

File:2pth.jpg

Template:STRUCTURE 2pth

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. 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 Sun May 4 13:46:45 2008

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