2pth

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:11, 21 February 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2pth.jpg|left|200px]]
 
-
<!--
+
==PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI==
-
The line below this paragraph, containing "STRUCTURE_2pth", creates the "Structure Box" on the page.
+
<StructureSection load='2pth' size='340' side='right'caption='[[2pth]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2pth]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PTH FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
-
-->
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pth OCA], [https://pdbe.org/2pth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pth RCSB], [https://www.ebi.ac.uk/pdbsum/2pth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pth ProSAT]</span></td></tr>
-
{{STRUCTURE_2pth| PDB=2pth | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PTH_ECOLI PTH_ECOLI] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Involved in lambda inhibition of host protein synthesis. PTH activity may, directly or indirectly, be the target for lambda bar RNA leading to rap cell death.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/2pth_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pth ConSurf].
 +
<div style="clear:both"></div>
-
'''PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI'''
+
==See Also==
-
 
+
*[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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.
+
[[Category: Escherichia coli K-12]]
-
 
+
[[Category: Large Structures]]
-
==About this Structure==
+
[[Category: Blanquet S]]
-
2PTH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTH OCA].
+
[[Category: Fromant M]]
-
 
+
[[Category: Mechulam Y]]
-
==Reference==
+
[[Category: Plateau P]]
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/9303320 9303320]
+
[[Category: Schmitt E]]
-
[[Category: Aminoacyl-tRNA hydrolase]]
+
-
[[Category: Escherichia coli]]
+
-
[[Category: Single protein]]
+
-
[[Category: Blanquet, S.]]
+
-
[[Category: Fromant, M.]]
+
-
[[Category: Mechulam, Y.]]
+
-
[[Category: Plateau, P.]]
+
-
[[Category: Schmitt, E.]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Peptidyl-trna]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:46:45 2008''
+

Current revision

PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI

PDB ID 2pth

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pth"
Personal tools