1vz3: Difference between revisions
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==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT== | ==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT== | ||
<StructureSection load='1vz3' size='340' side='right' caption='[[1vz3]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1vz3' size='340' side='right' caption='[[1vz3]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e5t|1e5t]], [[1e8m|1e8m]], [[1e8n|1e8n]], [[1h2w|1h2w]], [[1h2x|1h2x]], [[1h2y|1h2y]], [[1h2z|1h2z]], [[1o6f|1o6f]], [[1o6g|1o6g]], [[1qfm|1qfm]], [[1qfs|1qfs]], [[1uoo|1uoo]], [[1uop|1uop]], [[1uoq|1uoq]], [[1vz2|1vz2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e5t|1e5t]], [[1e8m|1e8m]], [[1e8n|1e8n]], [[1h2w|1h2w]], [[1h2x|1h2x]], [[1h2y|1h2y]], [[1h2z|1h2z]], [[1o6f|1o6f]], [[1o6g|1o6g]], [[1qfm|1qfm]], [[1qfs|1qfs]], [[1uoo|1uoo]], [[1uop|1uop]], [[1uoq|1uoq]], [[1vz2|1vz2]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vz3 OCA], [http://pdbe.org/1vz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vz3 RCSB], [http://www.ebi.ac.uk/pdbsum/1vz3 PDBsum]</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=1vz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vz3 OCA], [http://pdbe.org/1vz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vz3 RCSB], [http://www.ebi.ac.uk/pdbsum/1vz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vz3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/1vz3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/1vz3_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:15, 4 April 2018
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANTPROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT
Structural highlights
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 PubMedProlyl oligopeptidase contains a peptidase domain and its catalytic triad is covered by the central tunnel of a seven-bladed beta-propeller. This domain makes the enzyme an oligopeptidase by excluding large structured peptides from the active site. The apparently rigid crystal structure does not explain how the substrate can approach the catalytic groups. Two possibilities of substrate access were investigated: either blades 1 and 7 of the propeller domain move apart, or the peptidase and/or propeller domains move to create an entry site at the domain interface. Engineering disulfide bridges to the expected oscillating structures prevented such movements, which destroyed the catalytic activity and precluded substrate binding. This indicated that concerted movements of the propeller and the peptidase domains are essential for the enzyme action. Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding.,Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L J Mol Biol. 2004 Jul 9;340(3):627-37. PMID:15210359[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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