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1vz2

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Revision as of 13:28, 13 October 2021

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT

Structural highlights

1vz2 is a 1 chain structure with sequence from Pig. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1e5t, 1e8m, 1e8n, 1h2w, 1h2x, 1h2y, 1h2z, 1o6f, 1o6g, 1qfm, 1qfs, 1uoo, 1uop, 1uoq, 1vz3
Activity:	Prolyl oligopeptidase, with EC number 3.4.21.26
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 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.

References

↑ Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L. Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding. J Mol Biol. 2004 Jul 9;340(3):627-37. PMID:15210359 doi:10.1016/j.jmb.2004.05.011

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vz2"

@@ Line 3: / Line 3: @@
 <StructureSection load='1vz2' size='340' side='right'caption='[[1vz2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vz2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VZ2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vz2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZ2 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></td></tr>
+</td></tr><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>
-<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]], [[1vz3|1vz3]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]], [[1vz3|1vz3]]</div></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'>[https://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [https://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=1vz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vz2 OCA], [http://pdbe.org/1vz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1vz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vz2 ProSAT]</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=1vz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vz2 OCA], [https://pdbe.org/1vz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1vz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vz2 ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1vz2

From Proteopedia

Revision as of 13:28, 13 October 2021

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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