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| | <StructureSection load='1qfm' size='340' side='right'caption='[[1qfm]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='1qfm' size='340' side='right'caption='[[1qfm]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qfm]] is a 1 chain structure with 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=1QFM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QFM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qfm]] 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=1QFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SGL:1-HYDROXY-1-THIO-GLYCEROL'>SGL</scene>, <scene name='pdbligand=SGM:MONOTHIOGLYCEROL'>SGM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SGL:1-HYDROXY-1-THIO-GLYCEROL'>SGL</scene>, <scene name='pdbligand=SGM:MONOTHIOGLYCEROL'>SGM</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </span></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=1qfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfm OCA], [https://pdbe.org/1qfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfm RCSB], [https://www.ebi.ac.uk/pdbsum/1qfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfm ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfm OCA], [http://pdbe.org/1qfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qfm RCSB], [http://www.ebi.ac.uk/pdbsum/1qfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Prolyl oligopeptidase]] | |
| | [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| - | [[Category: Fulop, V]] | + | [[Category: Fulop V]] |
| - | [[Category: Alpha/beta-hydrolase]]
| + | |
| - | [[Category: Amnesia]]
| + | |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
1qfm is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.4Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PPCE_PIG Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fulop V, Bocskei Z, Polgar L. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell. 1998 Jul 24;94(2):161-70. PMID:9695945
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