2pth

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(New page: 200px<br /><applet load="2pth" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pth, resolution 1.2&Aring;" /> '''PEPTIDYL-TRNA HYDROLA...)
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[[Image:2pth.jpg|left|200px]]<br /><applet load="2pth" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pth, resolution 1.2&Aring;" />
 
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'''PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI==
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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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<StructureSection load='2pth' size='340' side='right'caption='[[2pth]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/2pth_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PTH OCA].
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*[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9303320 9303320]
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[[Category: Escherichia coli K-12]]
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[[Category: Aminoacyl-tRNA hydrolase]]
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[[Category: Large Structures]]
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[[Category: Escherichia coli]]
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[[Category: Blanquet S]]
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[[Category: Single protein]]
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[[Category: Fromant M]]
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[[Category: Blanquet, S.]]
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[[Category: Mechulam Y]]
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[[Category: Fromant, M.]]
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[[Category: Plateau P]]
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[[Category: Mechulam, Y.]]
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[[Category: Schmitt E]]
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[[Category: Plateau, P.]]
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[[Category: Schmitt, E.]]
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[[Category: hydrolase]]
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[[Category: peptidyl-trna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:39:39 2007''
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Current revision

PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI

PDB ID 2pth

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