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1a2z

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[[Image:1a2z.gif|left|200px]]<br /><applet load="1a2z" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a2z, resolution 1.73&Aring;" />
 
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'''PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS'''<br />
 
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==Overview==
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==PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS==
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BACKGROUND: Pyrrolidone carboxyl peptidases (pcps) are a group of, exopeptidases responsible for the hydrolysis of N-terminal pyroglutamate, residues from peptides and proteins. The bacterial and archaeal pcps are, members of a conserved family of cysteine proteases. The pcp from the, hyperthermophilic archaeon Thermococcus litoralis is more thermostable, than the bacterial enzymes with which it has up to 40% sequence identity., The pcp activity in archaea and eubacteria is proposed to be involved in, detoxification processes and in nutrient metabolism; eukaryotic, counterparts of the enzyme are involved in the processing of biologically, active peptides. RESULTS: The crystal structure of pcp has been determined, by multiple isomorphous replacement techniques at 1.73 A resolution and, refined to an R factor of 18.7% (Rfree = 21.4%). The enzyme is a, homotetramer of single open alpha/beta domain subunits, with a prominent, hydrophobic core formed from loops coming together from each monomer. The, active-site residues have been identified as a Cys143-His167-Glu80, catalytic triad. Structural homology to enzymes of different specificity, and mechanism has been identified. CONCLUSIONS: The Thermococcus pcp has, no sequence or structural homology with other members of the cysteine, protease family. It does, however, show considerable similarities to other, hydrolytic enzymes of widely varying substrate specificity and mechanism, suggesting that they are the products of divergent evolution from a common, ancestor. The enhanced thermostability of the T. litoralis pcp may arise, from hydrophobic interactions between the subunits and the presence of, intersubunit disulphide bridges.
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<StructureSection load='1a2z' size='340' side='right'caption='[[1a2z]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1a2z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2Z FirstGlance]. <br>
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1A2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pyroglutamyl-peptidase_I Pyroglutamyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.3 3.4.19.3] Known structural/functional Site: <scene name='pdbsite=AVE:Catalytic+Triad'>AVE</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2Z OCA].
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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]] 1.73&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1a2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2z OCA], [https://pdbe.org/1a2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2z RCSB], [https://www.ebi.ac.uk/pdbsum/1a2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2z ProSAT]</span></td></tr>
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X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis., Singleton M, Isupov M, Littlechild J, Structure. 1999 Mar 15;7(3):237-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368293 10368293]
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</table>
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[[Category: Pyroglutamyl-peptidase I]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/PCP_THELN PCP_THELN] Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
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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/a2/1a2z_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=1a2z ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermococcus litoralis]]
[[Category: Thermococcus litoralis]]
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[[Category: Isupov, M.N.]]
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[[Category: Isupov MN]]
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[[Category: Littlechild, J.A.]]
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[[Category: Littlechild JA]]
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[[Category: Singleton, M.R.]]
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[[Category: Singleton MR]]
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[[Category: SO4]]
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[[Category: n-pyroglutamate hydrolysis]]
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[[Category: peptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:28:49 2008''
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Current revision

PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS

PDB ID 1a2z

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