2pth
From Proteopedia
(New page: 200px<br /><applet load="2pth" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pth, resolution 1.2Å" /> '''PEPTIDYL-TRNA HYDROLA...) |
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| - | [[Image:2pth.jpg|left|200px]]<br /><applet load="2pth" size=" | + | [[Image:2pth.jpg|left|200px]]<br /><applet load="2pth" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2pth, resolution 1.2Å" /> | caption="2pth, resolution 1.2Å" /> | ||
'''PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI'''<br /> | '''PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptidyl-tRNA hydrolase activity from Escherichia coli ensures the | + | 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== | ==About this Structure== | ||
| - | 2PTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http:// | + | 2PTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peptidyl-trna]] | [[Category: peptidyl-trna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:48 2008'' |
Revision as of 16:32, 21 February 2008
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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
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