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1e5t

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(New page: 200px<br /> <applet load="1e5t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5t, resolution 1.7&Aring;" /> '''PROLYL OLIGOPEPTIDAS...)
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[[Image:1e5t.gif|left|200px]]<br />
 
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<applet load="1e5t" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e5t, resolution 1.7&Aring;" />
 
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'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT'''<br />
 
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==Overview==
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==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT==
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Proteases have a variety of strategies for selecting substrates in order, to prevent uncontrolled protein degradation. A recent crystal structure, determination of prolyl oligopeptidase has suggested a way for substrate, selection involving an unclosed seven-bladed beta-propeller domain. We, have engineered a disulfide bond between the first and seventh blades of, the propeller, which resulted in the loss of enzymatic activity. These, results provided direct evidence for a novel strategy of regulation in, which oscillating propeller blades act as a gating filter during, catalysis, letting small peptide substrates into the active site while, excluding large proteins to prevent accidental proteolysis.
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<StructureSection load='1e5t' size='340' side='right'caption='[[1e5t]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5T 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]] 1.7&#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=GOL:GLYCEROL'>GOL</scene></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=1e5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5t OCA], [https://pdbe.org/1e5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5t RCSB], [https://www.ebi.ac.uk/pdbsum/1e5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
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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/e5/1e5t_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=1e5t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis.
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==About this Structure==
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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.,Fulop V, Szeltner Z, Polgar L EMBO Rep. 2000 Sep;1(3):277-81. PMID:11256612<ref>PMID:11256612</ref>
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1E5T is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E5T OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism., Fulop V, Szeltner Z, Polgar L, EMBO Rep. 2000 Sep;1(3):277-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11256612 11256612]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1e5t" style="background-color:#fffaf0;"></div>
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[[Category: Sus scrofa]]
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[[Category: Fulop, V.]]
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[[Category: GOL]]
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[[Category: alpha/ beta-hydrolase]]
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[[Category: amnesia]]
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[[Category: beta-propeller]]
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[[Category: hydrolase]]
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[[Category: prolyl oligopeptidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:54:37 2007''
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==See Also==
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*[[Prolyl Endopeptidase|Prolyl Endopeptidase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sus scrofa]]
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[[Category: Fulop V]]

Current revision

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

PDB ID 1e5t

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