1vz3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:09, 13 December 2023) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1vz3.gif|left|200px]]<br />
 
-
<applet load="1vz3" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1vz3, resolution 1.6&Aring;" />
 
-
'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT'''<br />
 
-
==Overview==
+
==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT==
-
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.
+
<StructureSection load='1vz3' size='340' side='right'caption='[[1vz3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1vz3]] 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=1VZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZ3 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vz3 OCA], [https://pdbe.org/1vz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1vz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vz3 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<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>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1vz3 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
==About this Structure==
+
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<ref>PMID:15210359</ref>
-
1VZ3 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/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] Structure known Active Site: AS1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZ3 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15210359 15210359]
+
</div>
-
[[Category: Prolyl oligopeptidase]]
+
<div class="pdbe-citations 1vz3" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Sus scrofa]]
+
-
[[Category: Fulop, V.]]
+
-
[[Category: Rea, D.]]
+
-
[[Category: GOL]]
+
-
[[Category: alpha/ beta-hydrolase]]
+
-
[[Category: amnesia]]
+
-
[[Category: beta-propeller]]
+
-
[[Category: hydrolase]]
+
-
[[Category: prolyl oligopeptidase]]
+
-
[[Category: serine protease]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:20:27 2007''
+
==See Also==
 +
*[[Prolyl Endopeptidase|Prolyl Endopeptidase]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Sus scrofa]]
 +
[[Category: Fulop V]]
 +
[[Category: Rea D]]

Current revision

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT

PDB ID 1vz3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vz3"
Personal tools