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1qfs

From Proteopedia

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[[Image:1qfs.gif|left|200px]]
 
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==PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL==
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The line below this paragraph, containing "STRUCTURE_1qfs", creates the "Structure Box" on the page.
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<StructureSection load='1qfs' size='340' side='right'caption='[[1qfs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qfs]] 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=1QFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2&#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=ZPR:N-BENZYLOXYCARBONYL-L-PROLYL-L-PROLINAL'>ZPR</scene></td></tr>
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{{STRUCTURE_1qfs| PDB=1qfs | SCENE= }}
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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=1qfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfs OCA], [https://pdbe.org/1qfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfs RCSB], [https://www.ebi.ac.uk/pdbsum/1qfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfs 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/qf/1qfs_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=1qfs 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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Prolyl oligopeptidase is a large cytosolic enzyme that belongs to a new class of serine peptidases. The enzyme is involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The 1.4 A resolution crystal structure is presented here. The enzyme contains a peptidase domain with an alpha/beta hydrolase fold, and its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of an unusual beta propeller. This domain makes prolyl oligopeptidase an oligopeptidase by excluding large structured peptides from the active site. In this way, the propeller protects larger peptides and proteins from proteolysis in the cytosol. The structure is also obtained with a transition state inhibitor, which may facilitate drug design to treat memory disorders.
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'''PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL'''
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Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.,Fulop V, Bocskei Z, Polgar L Cell. 1998 Jul 24;94(2):161-70. PMID:9695945<ref>PMID:9695945</ref>
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==Overview==
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Prolyl oligopeptidase is a large cytosolic enzyme that belongs to a new class of serine peptidases. The enzyme is involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The 1.4 A resolution crystal structure is presented here. The enzyme contains a peptidase domain with an alpha/beta hydrolase fold, and its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of an unusual beta propeller. This domain makes prolyl oligopeptidase an oligopeptidase by excluding large structured peptides from the active site. In this way, the propeller protects larger peptides and proteins from proteolysis in the cytosol. The structure is also obtained with a transition state inhibitor, which may facilitate drug design to treat memory disorders.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1QFS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFS OCA].
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</div>
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<div class="pdbe-citations 1qfs" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis., Fulop V, Bocskei Z, Polgar L, Cell. 1998 Jul 24;94(2):161-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9695945 9695945]
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*[[Prolyl Endopeptidase|Prolyl Endopeptidase]]
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[[Category: Prolyl oligopeptidase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Fulop, V.]]
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[[Category: Fulop V]]
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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: Prolyl oligopeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:12:55 2008''
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Current revision

PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL

PDB ID 1qfs

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